Wikipedia

Proliferirajući ćelijski jedarni antigen

(Preusmjereno sa PCNA)

Proliferirajući ćelijski jedarni antigen (PCNA) je DNK-stezaljka koja djeluje kao procesivni faktor za DNK-polimerazu δ u eukariotske ćelije i neophodan je za replikaciju. PCNA je homotrimer i svoju procesnost postiže okružujući DNK, gdje djeluje kao skela za regrutovanje proteina uključenih u replikaciju DNK, popravak DNK, remodeliranje hromatina i epigenetičke uticaje. Kod ljudi, genski lokus PCNA nalazi se na kratkom (p) kraku hromosoma 20.[5]

PCNA
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

4D2G, 1AXC, 1U76, 1U7B, 1UL1, 1VYJ, 1VYM, 1W60, 2ZVK, 2ZVL, 2ZVM, 3P87, 3TBL, 3VKX, 3WGW, 4RJF, 3JA9, 4ZTD, 5IY4, 5E0U, 5E0T, 5E0V

Identifikatori
AliasiPCNA
Vanjski ID-jeviOMIM: 176740 MGI: 97503 HomoloGene: 1945 GeneCards: PCNA
Lokacija gena (čovjek)
Hromosom 20 (čovjek)
Hrom.Hromosom 20 (čovjek)[1]
Hromosom 20 (čovjek)
Genomska lokacija za PCNA
Genomska lokacija za PCNA
Bend20p12.3Početak5,114,953 bp[1]
Kraj5,126,626 bp[1]
Lokacija gena (miš)
Hromosom 2 (miš)
Hrom.Hromosom 2 (miš)[2]
Hromosom 2 (miš)
Genomska lokacija za PCNA
Genomska lokacija za PCNA
Bend2 F2|2 64.15 cMPočetak132,091,082 bp[2]
Kraj132,095,234 bp[2]
Obrazac RNK ekspresije
Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija• MutLalpha complex binding
• vezivanje identičnih proteina
• vezivanje enzima
• receptor tyrosine kinase binding
• vezivanje sa DNK
• DNA polymerase binding
• oštećeno vezivanje sa DNK
• dinucleotide insertion or deletion binding
• GO:0001948, GO:0016582 vezivanje za proteine
• chromatin binding
• histone acetyltransferase binding
• estrogen receptor binding
• purine-specific mismatch base pair DNA N-glycosylase activity
• DNA polymerase processivity factor activity
Ćelijska komponenta• jedro
• Replisom
• nukleoplazma
• Egzosom
• DNA replication factor C complex
• centrosom
• PCNA complex
• nuclear replication fork
• PCNA-p21 complex
• replication fork
• nuclear body
• Hromatin
Biološki proces• replication fork processing
• translesion synthesis
• Replikacija DNK
• nucleotide-excision repair, DNA gap filling
• protein sumoylation
• regulation of DNA replication
• transcription-coupled nucleotide-excision repair
• positive regulation of deoxyribonuclease activity
• nucleotide-excision repair, DNA incision
• error-free translesion synthesis
• GO:1900404 positive regulation of DNA repair
• regulation of transcription involved in G1/S transition of mitotic cell cycle
• positive regulation of DNA replication
• response to lipid
• heart development
• Popravak neusklađenosti DNK
• cellular response to DNA damage stimulus
• mitotic telomere maintenance via semi-conservative replication
• epithelial cell differentiation
• response to cadmium ion
• Ćelijska proliferacija
• telomere maintenance
• error-prone translesion synthesis
• cellular response to UV
• estrous cycle
• cellular response to hydrogen peroxide
• response to dexamethasone
• nucleotide-excision repair, DNA incision, 5'-to lesion
• liver regeneration
• response to estradiol
• GO:0001306 response to oxidative stress
• GO:0100026 Popravka DNK
• response to L-glutamate
• DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
• DNA ligation
• leading strand elongation
• protein ubiquitination
• telomere maintenance via semi-conservative replication
• GO:0022415 viral process
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez

5111

18538

Ensembl

ENSG00000132646

ENSMUSG00000027342

UniProt

P12004

P17918

RefSeq (mRNK)

NM_182649
NM_002592

NM_011045

RefSeq (bjelančevina)

NP_002583
NP_872590

NP_035175

Lokacija (UCSC)Chr 20: 5.11 – 5.13 MbChr 2: 132.09 – 132.1 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš
Cryo-EM struktura procesivnog kompleksa PolD–PCNA vezanog za DNK

Mnogi proteini stupaju u interakciju sa PCNA preko dva poznata PCNA-interagirajuća motiva PCNA-interaktivne peptidne (PIP) kutije [6] i AlkB homolog 2 PCNA motiva u interakciji (APIM).[7] Proteini koji se vezuju za PCNA preko PIP-kutije su uglavnom uključeni u replikaciju DNK, dok su proteini koji se vezuju za PCNA preko APIM-a uglavnom važni u kontekstu genotoksičnog stresa.[8]

Funkcija

uredi

Protein koji je kodiran ovim genom nalazi se u jedru i kofaktor je delta DNK-polimeraza. Kodirani protein djeluje kao homotrimer i pomaže u povećanju procesivnosti sinteze vodećeg lanca tokom replikacije DNK. Kao odgovor na oštećenje DNK, ovaj protein je ubikvitinski uključen, kao i u RAD6-ovisni put popravk DNK. Za ovaj gen su pronađene dvije varijante transkripta koje kodiraju isti protein. Pseudogeni ovog gena su opisani na hromosomu 4 i na hromosomu X.[9]

PCNA se također nalazi u arhejama, kao faktor procesivnosti polD, jedinstvene multifunkcionalne DNK-polimeraze u ovoj domeni života.[10]

Ekspresija u jedru tokom sinteze DNK

uredi

PCNA je prvobitno identifikovana kao antigen koji se eksprimira u ćelijskom jedru tokom faze sinteze DNK ćelijskog ciklusa. Dio proteina je sekvenciran i ta sekvenca je korištena da se omogući izolacija klona cDNK.[11] PCNA pomaže u držanju DNK-polimeraze delta (Pol δ) na DNK. PCNA je stegnut [12][13] koji je heteropentamerni član AAA+ klase ATPaza. Ekspresija PCNA je pod kontrolom kompleksa koji sadrže E2F transkripcijski faktor.[14][15]

Uloga u popravku DNK

uredi

Budući da je DNK-polimeraza epsilon uključena u resintezu izrezanih oštećenih lanaca DNK tokom popravka DNK, PCNA je važna i za sintezu DNK i za popravak DNK.[16][17]

PCNA je također uključen u put tolerancije oštećenja DNK poznat kao replikacijski popravak (PRR).[18] U PRR postoje dva potputa: (1) put translezije, koji se provodi specijaliziranim DNK-polimerazama koje su sposobne da inkorporiraju oštećene baze DNK u svoja aktivna mjesta (za razliku od normalne replikativne polimeraze, koja se zaustavlja), i time zaobilaze oštećenje, i (2) predloženi put "prebacivanja šablona" za koji se smatra da uključuje premoštavanje oštećenja angažovanjem mehanizma za homolognu rekombinaciju. PCNA je ključan za aktivaciju ovih puteva i izbor koji put će ćelija koristiti. PCNA postaje posttranslacijski modificiran pomoću ubikvitina.[19] Monoubikvitin lizina broj 164 na PCNA aktivira put sinteze translezije. Smatra se da proširenje ovog monoubikvitina pomoću nekanonskog lanca poliubikvitina vezanog uz lizin-63 na PCNA[19] aktivira put prebacivanja šablona. Nadalje, sumoilacija (pomoću malog modifikatora sličnog ubikvitinu, SUMO) PCNA lizina-164 (i u manjoj mjeri, lizina-127) inhibira put prebacivanja šablona.[19] Ovaj antagonistički efekt nastaje jer sumoilirana PCNA regrutuje DNK-helikazu zvanu Srs2,[20] koja ima ulogu u razbijanju Rad51 nukleoproteinskih filamenata koji su fundamentalni za iniciranje homologne rekombinacije.

PCNA-vezujući proteini

uredi

PCNA stupa u interakciju s mnogim proteinima.[21]

Interakcije

uredi

Pokazalo se da PCNA interraguje sa:

Proteini koji komuniciraju sa PCNA preko APIM-a uključuju ljudski AlkB homolog 2, TFIIS-L, TFII-I, Rad51B,[7] XPA,[87] ZRANB3,[88] and FBH1.[89]

Upotreba

uredi

Antitijela protiv proliferirajućeg ćelijskog jedarnog antigena (PCNA) ili monoklonsko antitijelo zvano Ki-67 može se koristiti za procjenu različitih neoplazmi, npr. astrocitoma. Mogu imati dijagnostičku i prognostičku vrijednost. Snimanje jedarne distribucije PCNA (putem označavanja antitijela) može se koristiti za razlikovanje između ranog, srednje i kasne S-faze ćelijskog ciklusa.[90] Međutim, važno ograničenje antitijela je da ćelije moraju biti fiksirane što dovodi do potencijalnih artefakata.

S druge strane, proučavanje dinamike replikacije i popravke u živim ćelijama može se obaviti uvođenjem translacijskih fuzija PCNA. Da bi se eliminisala potreba za transfekcijama i zaobišao problem ćelija koje je teško transficirati i/ili kratko žive, mogu se koristiti markeri za replikaciju i/ili reparaciju permeabilnih ćelija. Ovi peptidi nude izrazitu prednost koja se može koristiti "in situ" u živom tkivu i čak razlikovati ćelije koje su podvrgnute replikaciji od ćelija koje su podvrgnute popravljanju..[91]

PCNA je potencijalna terapijska meta u terapiji kancera.[92]

Također pogledajte

uredi

Reference

uredi
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000132646 - Ensembl, maj 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027342 - Ensembl, maj 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Moldovan GL, Pfander B, Jentsch S (18. 5. 2007). "PCNA, the maestro of the replication fork". Cell. 129 (4): 665–79. doi:10.1016/j.cell.2007.05.003. PMID 17512402. S2CID 3547069.
  6. ^ Warbrick E (Mar 1998). "PCNA binding through a conserved motif". BioEssays. 20 (3): 195–9. doi:10.1002/(sici)1521-1878(199803)20:3<195::aid-bies2>3.0.co;2-r. PMID 9631646.
  7. ^ a b Gilljam KM, Feyzi E, Aas PA, Sousa MM, Müller R, Vågbø CB, Catterall TC, Liabakk NB, Slupphaug G, Drabløs F, Krokan HE, Otterlei M (Sep 7, 2009). "Identification of a novel, widespread, and functionally important PCNA-binding motif". The Journal of Cell Biology. 186 (5): 645–54. doi:10.1083/jcb.200903138. PMC 2742182. PMID 19736315.
  8. ^ Mailand N, Gibbs-Seymour I, Bekker-Jensen S (maj 2013). "Regulation of PCNA-protein interactions for genome stability". Nature Reviews Molecular Cell Biology. 14 (5): 269–82. doi:10.1038/nrm3562. PMID 23594953. S2CID 25952152.
  9. ^ "Entrez Gene: PCNA proliferating cell nuclear antigen".
  10. ^ Madru C, Henneke G, Raia P, Hugonneau-Beaufet I, Pehau-Arnaudet G, England P, et al. (mart 2020). "Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA". Nature Communications. 11 (1): 1591. Bibcode:2020NatCo..11.1591M. doi:10.1038/s41467-020-15392-9. PMC 7101311. PMID 32221299.
  11. ^ Matsumoto K, Moriuchi T, Koji T, Nakane PK (1987). "Molecular cloning of cDNA coding for rat proliferating cell nuclear antigen (PCNA)/cyclin". EMBO J. 6 (3): 637–42. doi:10.1002/j.1460-2075.1987.tb04802.x. PMC 553445. PMID 2884104.[mrtav link]
  12. ^ Bowman GD, O'Donnell M, Kuriyan J (2004). "Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex". Nature. 429 (6993): 724–730. Bibcode:2004Natur.429..724B. doi:10.1038/nature02585. PMID 15201901. S2CID 4346799.
  13. ^ Zhang G, Gibbs E, Kelman Z, O'Donnell M, Hurwitz J (1999). "Studies on the interactions between human replication factor C and human proliferating cell nuclear antigen". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 1869–1874. Bibcode:1999PNAS...96.1869Z. doi:10.1073/pnas.96.5.1869. PMC 26703. PMID 10051561.
  14. ^ Egelkrout EM, Mariconti L, Settlage SB, Cella R, Robertson D, Hanley-Bowdoin L (2002). "Two E2F elements regulate the proliferating cell nuclear antigen promoter differently during leaf development". Plant Cell. 14 (12): 3225–3236. doi:10.1105/tpc.006403. PMC 151214. PMID 12468739.
  15. ^ Nikolai BC, Lanz RB, York B, Dasgupta S, Mitsiades N, Creighton CJ, Tsimelzon A, Hilsenbeck SG, Lonard DM, Smith CL, O'Malley BW (15. 3. 2016). "HER2 Signaling Drives DNA Anabolism and Proliferation through SRC-3 Phosphorylation and E2F1-Regulated Genes". Cancer Res. 76 (6): 1463–75. doi:10.1158/0008-5472.CAN-15-2383. PMC 4794399. PMID 26833126.
  16. ^ Shivji KK, Kenny MK, Wood RD (april 1992). "Proliferating cell nuclear antigen is required for DNA excision repair". Cell. 69 (2): 367–74. doi:10.1016/0092-8674(92)90416-A. PMID 1348971. S2CID 12260457.
  17. ^ Essers J, Theil AF, Baldeyron C, van Cappellen WA, Houtsmuller AB, Kanaar R, Vermeulen W (2005). "Nuclear dynamics of PCNA in DNA replication and repair". Mol. Cell. Biol. 25 (21): 9350–9359. doi:10.1128/MCB.25.21.9350-9359.2005. PMC 1265825. PMID 16227586.
  18. ^ Lehmann AR, Fuchs RP (decembar 2006). "Gaps and forks in DNA replication: Rediscovering old models" (PDF). DNA Repair (Amst.). 5 (12): 1495–1498. doi:10.1016/j.dnarep.2006.07.002. PMID 16956796.
  19. ^ a b c Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S (septembar 2002). "RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO". Nature. 419 (6903): 135–141. Bibcode:2002Natur.419..135H. doi:10.1038/nature00991. PMID 12226657. S2CID 205209495.
  20. ^ Pfander B, Moldovan GL, Sacher M, Hoege C, Jentsch S (juli 2005). "SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase". Nature. 436 (7049): 428–33. Bibcode:2005Natur.436..428P. doi:10.1038/nature03665. PMID 15931174. S2CID 4316517.
  21. ^ Moldovan GL, Pfander B, Jentsch S (2007). "PCNA, the maestro of the replication fork". Cell. 129 (4): 665–679. doi:10.1016/j.cell.2007.05.003. PMID 17512402. S2CID 3547069.
  22. ^ Witko-Sarsat V, Mocek J, Bouayad D, Tamassia N, Ribeil JA, Candalh C, Davezac N, Reuter N, Mouthon L, Hermine O, Pederzoli-Ribeil M, Cassatella MA (Nov 22, 2010). "Proliferating cell nuclear antigen acts as a cytoplasmic platform controlling human neutrophil survival". The Journal of Experimental Medicine. 207 (12): 2631–45. doi:10.1084/jem.20092241. PMC 2989777. PMID 20975039.
  23. ^ a b c d e f g h i j k l m Ohta S, Shiomi Y, Sugimoto K, Obuse C, Tsurimoto T (oktobar 2002). "A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein". J. Biol. Chem. 277 (43): 40362–7. doi:10.1074/jbc.M206194200. PMID 12171929.
  24. ^ Zhang K, Gao Y, Li J, Burgess R, Han J, Liang H, Zhang Z, Liu Y (juni 2016). "A DNA binding winged helix domain in CAF-1 functions with PCNA to stabilize CAF-1 at replication forks". Nucleic Acids Research. 44 (11): 5083–94. doi:10.1093/nar/gkw106. PMC 4914081. PMID 26908650.
  25. ^ Moggs JG, Grandi P, Quivy JP, Jónsson ZO, Hübscher U, Becker PB, Almouzni G (februar 2000). "A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing DNA damage". Molecular and Cellular Biology. 20 (4): 1206–18. doi:10.1128/mcb.20.4.1206-1218.2000. PMC 85246. PMID 10648606.
  26. ^ Rolef Ben-Shahar T, Castillo AG, Osborne MJ, Borden KL, Kornblatt J, Verreault A (decembar 2009). "Two fundamentally distinct PCNA interaction peptides contribute to chromatin assembly factor 1 function". Molecular and Cellular Biology. 29 (24): 6353–65. doi:10.1128/MCB.01051-09. PMC 2786881. PMID 19822659.
  27. ^ Kawabe T, Suganuma M, Ando T, Kimura M, Hori H, Okamoto T (mart 2002). "Cdc25C interacts with PCNA at G2/M transition". Oncogene. 21 (11): 1717–26. doi:10.1038/sj.onc.1205229. PMID 11896603.
  28. ^ Matsuoka S, Yamaguchi M, Matsukage A (april 1994). "D-type cyclin-binding regions of proliferating cell nuclear antigen". J. Biol. Chem. 269 (15): 11030–6. doi:10.1016/S0021-9258(19)78087-9. PMID 7908906.
  29. ^ a b Xiong Y, Zhang H, Beach D (august 1993). "Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation". Genes Dev. 7 (8): 1572–83. doi:10.1101/gad.7.8.1572. PMID 8101826.
  30. ^ Otterlei M, Warbrick E, Nagelhus TA, Haug T, Slupphaug G, Akbari M, Aas PA, Steinsbekk K, Bakke O, Krokan HE (juli 1999). "Post-replicative base excision repair in replication foci". EMBO J. 18 (13): 3834–44. doi:10.1093/emboj/18.13.3834. PMC 1171460. PMID 10393198.
  31. ^ Serrano M, Hannon GJ, Beach D (decembar 1993). "A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4". Nature. 366 (6456): 704–7. Bibcode:1993Natur.366..704S. doi:10.1038/366704a0. PMID 8259215. S2CID 4368128.
  32. ^ a b Watanabe H, Pan ZQ, Schreiber-Agus N, DePinho RA, Hurwitz J, Xiong Y (februar 1998). "Suppression of cell transformation by the cyclin-dependent kinase inhibitor p57KIP2 requires binding to proliferating cell nuclear antigen". Proc. Natl. Acad. Sci. U.S.A. 95 (4): 1392–7. Bibcode:1998PNAS...95.1392W. doi:10.1073/pnas.95.4.1392. PMC 19016. PMID 9465025.
  33. ^ Rountree MR, Bachman KE, Baylin SB (juli 2000). "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci". Nat. Genet. 25 (3): 269–77. doi:10.1038/77023. PMID 10888872. S2CID 26149386.
  34. ^ Iida T, Suetake I, Tajima S, Morioka H, Ohta S, Obuse C, Tsurimoto T (oktobar 2002). "PCNA clamp facilitates action of DNA cytosine methyltransferase 1 on hemimethylated DNA". Genes Cells. 7 (10): 997–1007. doi:10.1046/j.1365-2443.2002.00584.x. PMID 12354094. S2CID 25310911.
  35. ^ Chuang LS, Ian HI, Koh TW, Ng HH, Xu G, Li BF (septembar 1997). "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for p21WAF1". Science. 277 (5334): 1996–2000. doi:10.1126/science.277.5334.1996. PMID 9302295.
  36. ^ Hasan S, Hassa PO, Imhof R, Hottiger MO (mart 2001). "Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis". Nature. 410 (6826): 387–91. Bibcode:2001Natur.410..387H. doi:10.1038/35066610. PMID 11268218. S2CID 2129847.
  37. ^ Bender D, De Silva E, Chen J, Poss A, Gawey L, Rulon Z, Rankin, S (decembar 2019). "Multivalent interaction of ESCO2 with replication machinery is required for sister chromatid cohesion in vertebrates". Proc. Natl. Acad. Sci. U.S.A. 117 (2): 1081–1089. doi:10.1073/pnas.1911936117. PMC 6969535. PMID 31879348.
  38. ^ Henneke G, Koundrioukoff S, Hübscher U (juli 2003). "Phosphorylation of human Fen1 by cyclin-dependent kinase modulates its role in replication fork regulation". Oncogene. 22 (28): 4301–13. doi:10.1038/sj.onc.1206606. PMID 12853968.
  39. ^ Hasan S, Stucki M, Hassa PO, Imhof R, Gehrig P, Hunziker P, Hübscher U, Hottiger MO (juni 2001). "Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300". Mol. Cell. 7 (6): 1221–31. doi:10.1016/s1097-2765(01)00272-6. PMID 11430825.
  40. ^ a b Jónsson ZO, Hindges R, Hübscher U (april 1998). "Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen". EMBO J. 17 (8): 2412–25. doi:10.1093/emboj/17.8.2412. PMC 1170584. PMID 9545252.
  41. ^ Gary R, Ludwig DL, Cornelius HL, MacInnes MA, Park MS (septembar 1997). "The DNA repair endonuclease XPG binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding regions of FEN-1 and cyclin-dependent kinase inhibitor p21". J. Biol. Chem. 272 (39): 24522–9. doi:10.1074/jbc.272.39.24522. PMID 9305916.
  42. ^ Chen U, Chen S, Saha P, Dutta A (oktobar 1996). "p21Cip1/Waf1 disrupts the recruitment of human Fen1 by proliferating-cell nuclear antigen into the DNA replication complex". Proc. Natl. Acad. Sci. U.S.A. 93 (21): 11597–602. Bibcode:1996PNAS...9311597C. doi:10.1073/pnas.93.21.11597. PMC 38103. PMID 8876181.
  43. ^ Dianova II, Bohr VA, Dianov GL (oktobar 2001). "Interaction of human AP endonuclease 1 with flap endonuclease 1 and proliferating cell nuclear antigen involved in long-patch base excision repair". Biochemistry. 40 (42): 12639–44. doi:10.1021/bi011117i. PMID 11601988.
  44. ^ a b c Yu P, Huang B, Shen M, Lau C, Chan E, Michel J, Xiong Y, Payan DG, Luo Y (januar 2001). "p15(PAF), a novel PCNA associated factor with increased expression in tumor tissues". Oncogene. 20 (4): 484–9. doi:10.1038/sj.onc.1204113. PMID 11313979.
  45. ^ Smith ML, Chen IT, Zhan Q, Bae I, Chen CY, Gilmer TM, Kastan MB, O'Connor PM, Fornace AJ (novembar 1994). "Interaction of the p53-regulated protein Gadd45 with proliferating cell nuclear antigen". Science (Submitted manuscript). 266 (5189): 1376–80. Bibcode:1994Sci...266.1376S. doi:10.1126/science.7973727. PMID 7973727.
  46. ^ Chen IT, Smith ML, O'Connor PM, Fornace AJ (novembar 1995). "Direct interaction of Gadd45 with PCNA and evidence for competitive interaction of Gadd45 and p21Waf1/Cip1 with PCNA". Oncogene. 11 (10): 1931–7. PMID 7478510.
  47. ^ Vairapandi M, Azam N, Balliet AG, Hoffman B, Liebermann DA (juni 2000). "Characterization of MyD118, Gadd45, and proliferating cell nuclear antigen (PCNA) interacting domains. PCNA impedes MyD118 AND Gadd45-mediated negative growth control". J. Biol. Chem. 275 (22): 16810–9. doi:10.1074/jbc.275.22.16810. PMID 10828065.
  48. ^ Hall PA, Kearsey JM, Coates PJ, Norman DG, Warbrick E, Cox LS (juni 1995). "Characterisation of the interaction between PCNA and Gadd45". Oncogene. 10 (12): 2427–33. PMID 7784094.
  49. ^ Yang Q, Manicone A, Coursen JD, Linke SP, Nagashima M, Forgues M, Wang XW (novembar 2000). "Identification of a functional domain in a GADD45-mediated G2/M checkpoint". J. Biol. Chem. 275 (47): 36892–8. doi:10.1074/jbc.M005319200. PMID 10973963.
  50. ^ Azam N, Vairapandi M, Zhang W, Hoffman B, Liebermann DA (januar 2001). "Interaction of CR6 (GADD45gamma ) with proliferating cell nuclear antigen impedes negative growth control". J. Biol. Chem. 276 (4): 2766–74. doi:10.1074/jbc.M005626200. PMID 11022036.
  51. ^ Nakayama K, Hara T, Hibi M, Hirano T, Miyajima A (august 1999). "A novel oncostatin M-inducible gene OIG37 forms a gene family with MyD118 and GADD45 and negatively regulates cell growth". J. Biol. Chem. 274 (35): 24766–72. doi:10.1074/jbc.274.35.24766. PMID 10455148.
  52. ^ Milutinovic S, Zhuang Q, Szyf M (juni 2002). "Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification". J. Biol. Chem. 277 (23): 20974–8. doi:10.1074/jbc.M202504200. PMID 11929879.
  53. ^ Komatsu K, Wharton W, Hang H, Wu C, Singh S, Lieberman HB, Pledger WJ, Wang HG (novembar 2000). "PCNA interacts with hHus1/hRad9 in response to DNA damage and replication inhibition". Oncogene. 19 (46): 5291–7. doi:10.1038/sj.onc.1203901. PMID 11077446.
  54. ^ Scott M, Bonnefin P, Vieyra D, Boisvert FM, Young D, Bazett-Jones DP, Riabowol K (oktobar 2001). "UV-induced binding of ING1 to PCNA regulates the induction of apoptosis". J. Cell Sci. 114 (Pt 19): 3455–62. doi:10.1242/jcs.114.19.3455. PMID 11682605.
  55. ^ He H, Tan CK, Downey KM, So AG (oktobar 2001). "A tumor necrosis factor alpha- and interleukin 6-inducible protein that interacts with the small subunit of DNA polymerase delta and proliferating cell nuclear antigen". Proc. Natl. Acad. Sci. U.S.A. 98 (21): 11979–84. Bibcode:2001PNAS...9811979H. doi:10.1073/pnas.221452098. PMC 59753. PMID 11593007.
  56. ^ a b Balajee AS, Geard CR (mart 2001). "Chromatin-bound PCNA complex formation triggered by DNA damage occurs independent of the ATM gene product in human cells". Nucleic Acids Res. 29 (6): 1341–51. doi:10.1093/nar/29.6.1341. PMC 29758. PMID 11239001.
  57. ^ Matheos D, Ruiz MT, Price GB, Zannis-Hadjopoulos M (oktobar 2002). "Ku antigen, an origin-specific binding protein that associates with replication proteins, is required for mammalian DNA replication". Biochim. Biophys. Acta. 1578 (1–3): 59–72. doi:10.1016/s0167-4781(02)00497-9. PMID 12393188.
  58. ^ Fujise K, Zhang D, Liu J, Yeh ET (decembar 2000). "Regulation of apoptosis and cell cycle progression by MCL1. Differential role of proliferating cell nuclear antigen". J. Biol. Chem. 275 (50): 39458–65. doi:10.1074/jbc.M006626200. PMID 10978339.
  59. ^ a b Kleczkowska HE, Marra G, Lettieri T, Jiricny J (mart 2001). "hMSH3 and hMSH6 interact with PCNA and colocalize with it to replication foci". Genes Dev. 15 (6): 724–36. doi:10.1101/gad.191201. PMC 312660. PMID 11274057.
  60. ^ a b Clark AB, Valle F, Drotschmann K, Gary RK, Kunkel TA (novembar 2000). "Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes". J. Biol. Chem. 275 (47): 36498–501. doi:10.1074/jbc.C000513200. PMID 11005803.
  61. ^ Parker A, Gu Y, Mahoney W, Lee SH, Singh KK, Lu AL (februar 2001). "Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair". J. Biol. Chem. 276 (8): 5547–55. doi:10.1074/jbc.M008463200. PMID 11092888.
  62. ^ a b Fotedar R, Mossi R, Fitzgerald P, Rousselle T, Maga G, Brickner H, Messier H, Kasibhatla S, Hübscher U, Fotedar A (august 1996). "A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells". EMBO J. 15 (16): 4423–33. doi:10.1002/j.1460-2075.1996.tb00815.x. PMC 452166. PMID 8861969.
  63. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (oktobar 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  64. ^ Frouin I, Maga G, Denegri M, Riva F, Savio M, Spadari S, Prosperi E, Scovassi AI (oktobar 2003). "Human proliferating cell nuclear antigen, poly(ADP-ribose) polymerase-1, and p21waf1/cip1. A dynamic exchange of partners". J. Biol. Chem. 278 (41): 39265–8. doi:10.1074/jbc.C300098200. PMID 12930846.
  65. ^ Gulbis JM, Kelman Z, Hurwitz J, O'Donnell M, Kuriyan J (oktobar 1996). "Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA". Cell. 87 (2): 297–306. doi:10.1016/s0092-8674(00)81347-1. PMID 8861913. S2CID 17461501.
  66. ^ Touitou R, Richardson J, Bose S, Nakanishi M, Rivett J, Allday MJ (maj 2001). "A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome". EMBO J. 20 (10): 2367–75. doi:10.1093/emboj/20.10.2367. PMC 125454. PMID 11350925.
  67. ^ Lu X, Tan CK, Zhou JQ, You M, Carastro LM, Downey KM, So AG (juli 2002). "Direct interaction of proliferating cell nuclear antigen with the small subunit of DNA polymerase delta". J. Biol. Chem. 277 (27): 24340–5. doi:10.1074/jbc.M200065200. PMID 11986310.
  68. ^ Ducoux M, Urbach S, Baldacci G, Hübscher U, Koundrioukoff S, Christensen J, Hughes P (decembar 2001). "Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA replication through a conserved p21(Cip1)-like PCNA-binding motif present in the third subunit of human DNA polymerase delta". J. Biol. Chem. 276 (52): 49258–66. doi:10.1074/jbc.M106990200. PMID 11595739.
  69. ^ Liu L, Rodriguez-Belmonte EM, Mazloum N, Xie B, Lee MY (mart 2003). "Identification of a novel protein, PDIP38, that interacts with the p50 subunit of DNA polymerase delta and proliferating cell nuclear antigen". J. Biol. Chem. 278 (12): 10041–7. doi:10.1074/jbc.M208694200. PMID 12522211.
  70. ^ Haracska L, Johnson RE, Unk I, Phillips B, Hurwitz J, Prakash L, Prakash S (novembar 2001). "Physical and functional interactions of human DNA polymerase eta with PCNA". Mol. Cell. Biol. 21 (21): 7199–206. doi:10.1128/MCB.21.21.7199-7206.2001. PMC 99895. PMID 11585903.
  71. ^ Haracska L, Unk I, Johnson RE, Phillips BB, Hurwitz J, Prakash L, Prakash S (februar 2002). "Stimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA". Mol. Cell. Biol. 22 (3): 784–91. doi:10.1128/mcb.22.3.784-791.2002. PMC 133560. PMID 11784855.
  72. ^ Maga G, Villani G, Ramadan K, Shevelev I, Tanguy Le Gac N, Blanco L, Blanca G, Spadari S, Hübscher U (decembar 2002). "Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis". J. Biol. Chem. 277 (50): 48434–40. doi:10.1074/jbc.M206889200. PMID 12368291.
  73. ^ Shimazaki N, Yoshida K, Kobayashi T, Toji S, Tamai K, Koiwai O (juli 2002). "Over-expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme". Genes Cells. 7 (7): 639–51. doi:10.1046/j.1365-2443.2002.00547.x. PMID 12081642. S2CID 29714829.
  74. ^ Maruyama T, Farina A, Dey A, Cheong J, Bermudez VP, Tamura T, Sciortino S, Shuman J, Hurwitz J, Ozato K (septembar 2002). "A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase". Mol. Cell. Biol. 22 (18): 6509–20. doi:10.1128/mcb.22.18.6509-6520.2002. PMC 135621. PMID 12192049.
  75. ^ a b Mossi R, Jónsson ZO, Allen BL, Hardin SH, Hübscher U (januar 1997). "Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen". J. Biol. Chem. 272 (3): 1769–76. doi:10.1074/jbc.272.3.1769. PMID 8999859.
  76. ^ van der Kuip H, Carius B, Haque SJ, Williams BR, Huber C, Fischer T (april 1999). "The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G1 phase cell cycle regulatory proteins". J. Mol. Med. 77 (4): 386–92. doi:10.1007/s001090050365. PMID 10353443. S2CID 22183443.
  77. ^ a b c Cai J, Gibbs E, Uhlmann F, Phillips B, Yao N, O'Donnell M, Hurwitz J (juli 1997). "A complex consisting of human replication factor C p40, p37, and p36 subunits is a DNA-dependent ATPase and an intermediate in the assembly of the holoenzyme". J. Biol. Chem. 272 (30): 18974–81. doi:10.1074/jbc.272.30.18974. PMID 9228079.
  78. ^ Pan ZQ, Chen M, Hurwitz J (januar 1993). "The subunits of activator 1 (replication factor C) carry out multiple functions essential for proliferating-cell nuclear antigen-dependent DNA synthesis". Proc. Natl. Acad. Sci. U.S.A. 90 (1): 6–10. Bibcode:1993PNAS...90....6P. doi:10.1073/pnas.90.1.6. PMC 45588. PMID 8093561.
  79. ^ Merkle CJ, Karnitz LM, Henry-Sánchez JT, Chen J (august 2003). "Cloning and characterization of hCTF18, hCTF8, and hDCC1. Human homologs of a Saccharomyces cerevisiae complex involved in sister chromatid cohesion establishment". J. Biol. Chem. 278 (32): 30051–6. doi:10.1074/jbc.M211591200. PMID 12766176.
  80. ^ Motegi A, Liaw HJ, Lee KY, Roest HP, Maas A, Wu X, Moinova H, Markowitz SD, Ding H, Hoeijmakers JH, Myung K (august 2008). "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks". Proc. Natl. Acad. Sci. U.S.A. 105 (34): 12411–6. Bibcode:2008PNAS..10512411M. doi:10.1073/pnas.0805685105. PMC 2518831. PMID 18719106.
  81. ^ Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L (mart 2008). "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination". Proc. Natl. Acad. Sci. U.S.A. 105 (10): 3768–73. Bibcode:2008PNAS..105.3768U. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726.
  82. ^ Brun J, Chiu R, Lockhart K, Xiao W, Wouters BG, Gray DA (2008). "hMMS2 serves a redundant role in human PCNA polyubiquitination". BMC Mol. Biol. 9: 24. doi:10.1186/1471-2199-9-24. PMC 2263069. PMID 18284681.
  83. ^ Rodríguez-López AM, Jackson DA, Nehlin JO, Iborra F, Warren AV, Cox LS (februar 2003). "Characterisation of the interaction between WRN, the helicase/exonuclease defective in progeroid Werner's syndrome, and an essential replication factor, PCNA". Mech. Ageing Dev. 124 (2): 167–74. doi:10.1016/s0047-6374(02)00131-8. PMID 12633936. S2CID 37287691.
  84. ^ Huang S, Beresten S, Li B, Oshima J, Ellis NA, Campisi J (juni 2000). "Characterization of the human and mouse WRN 3'-->5' exonuclease". Nucleic Acids Res. 28 (12): 2396–405. doi:10.1093/nar/28.12.2396. PMC 102739. PMID 10871373.
  85. ^ Fan J, Otterlei M, Wong HK, Tomkinson AE, Wilson DM (2004). "XRCC1 co-localizes and physically interacts with PCNA". Nucleic Acids Res. 32 (7): 2193–201. doi:10.1093/nar/gkh556. PMC 407833. PMID 15107487.
  86. ^ Ise T, Nagatani G, Imamura T, Kato K, Takano H, Nomoto M, Izumi H, Ohmori H, Okamoto T, Ohga T, Uchiumi T, Kuwano M, Kohno K (januar 1999). "Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating cell nuclear antigen". Cancer Res. 59 (2): 342–6. PMID 9927044.
  87. ^ Gilljam KM, Müller R, Liabakk NB, Otterlei M (2012). "Nucleotide excision repair is associated with the replisome and its efficiency depends on a direct interaction between XPA and PCNA". PLOS ONE. 7 (11): e49199. Bibcode:2012PLoSO...749199G. doi:10.1371/journal.pone.0049199. PMC 3496702. PMID 23152873.
  88. ^ Ciccia A, Nimonkar AV, Hu Y, Hajdu I, Achar YJ, Izhar L, Petit SA, Adamson B, Yoon JC, Kowalczykowski SC, Livingston DM, Haracska L, Elledge SJ (Aug 10, 2012). "Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain genomic integrity after replication stress". Molecular Cell. 47 (3): 396–409. doi:10.1016/j.molcel.2012.05.024. PMC 3613862. PMID 22704558.
  89. ^ Bacquin A, Pouvelle C, Siaud N, Perderiset M, Salomé-Desnoulez S, Tellier-Lebegue C, Lopez B, Charbonnier JB, Kannouche PL (Jul 2013). "The helicase FBH1 is tightly regulated by PCNA via CRL4(Cdt2)-mediated proteolysis in human cells". Nucleic Acids Research. 41 (13): 6501–13. doi:10.1093/nar/gkt397. PMC 3711418. PMID 23677613.
  90. ^ Schönenberger F, Deutzmann A, Ferrando-May E, Merhof D (29. 5. 2015). "Discrimination of cell cycle phases in PCNA-immunolabeled cells". BMC Bioinform. 16 (180): 180. doi:10.1186/s12859-015-0618-9. PMC 4448323. PMID 26022740.
  91. ^ Herce HD, Rajan M, Lättig-Tünnemann G, Fillies M, Cardoso MC (3. 9. 2014). "A novel cell permeable DNA replication and repair marker". Nucleus (Austin, Tex.). 5 (6): 590–600. doi:10.4161/nucl.36290. PMC 4615156. PMID 25484186.
  92. ^ Wang SC (Apr 2014). "PCNA: a silent housekeeper or a potential therapeutic target?". Trends in Pharmacological Sciences. 35 (4): 178–186. doi:10.1016/j.tips.2014.02.004. PMID 24655521.

Dopunska literatura

uredi

Vanjski linkovi

uredi
Preuzeto iz "https://bs.wikipedia.org/w/index.php?title=Proliferirajući_ćelijski_jedarni_antigen&oldid=3673457"