MTERF
Mitohondrijskoterminacjski faktor transkripcije 1, znan i kao aMTERF1, jest protein koji je kod ljudi kodiran genom MTERF.[5][6][7][8]
Aminokiselinska sekvenca
urediDužina polipeptidnog lanca je 399 aminokiselina, а molekulska težina 45.778 Da.[9]
| 10 | 20 | 30 | 40 | 50 | ||||
|---|---|---|---|---|---|---|---|---|
| MQSLSLGQTS | ISKGLNYLTI | MAPGNLWHMR | NNFLFGSRCW | MTRFSAENIF | ||||
| KSVSFRLFGV | KCHNTDSEPL | KNEDLLKNLL | TMGVDIDMAR | KRQPGVFHRM | ||||
| ITNEQDLKMF | LLSKGASKEV | IASIISRYPR | AITRTPENLS | KRWDLWRKIV | ||||
| TSDLEIVNIL | ERSPESFFRS | NNNLNLENNI | KFLYSVGLTR | KCLCRLLTNA | ||||
| PRTFSNSLDL | NKQMVEFLQA | AGLSLGHNDP | ADFVRKIIFK | NPFILIQSTK | ||||
| RVKANIEFLR | STFNLNSEEL | LVLICGPGAE | ILDLSNDYAR | RSYANIKEKL | ||||
| FSLGCTEEEV | QKFVLSYPDV | IFLAEKKFND | KIDCLMEENI | SISQIIENPR | ||||
| VLDSSISTLK | SRIKELVNAG | CNLSTLNITL | LSWSKKRYEA | KLKKLSRFA |
Funkcija
urediOvaj gen kodira transkripciju terminacijskog faktora u mitohondrijama. Protein učestvuje u slabljenju transkripcije iz mitohondrijskog genoma; ovo slabljenje omogućava veće nivoe ekspresije 16S ribosomske RNK u odnosu na nizvodni gen za tRNK. Proizvod ovog gena ima tri motiva leucinskog zatvarača koji su u pregradama povezani s dva osnovna domena koji su oba potrebna za vezivanje DNK. Postoje dokazi da za ovaj protein zatvarači sudjeluju u intramolekulnim interakcijama koje uspostavljaju trodimenzijsku strukturu potrebnu za vezanje DNK.[5]
Reference
uredi- ^ a b c GRCh38: Ensembl release 89: ENSG00000127989 - Ensembl, maj 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000053178 - Ensembl, maj 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b "Entrez Gene: MTERF mitochondrial transcription termination factor".
- ^ Daga A, Micol V, Hess D, Aebersold R, Attardi G (april 1993). "Molecular characterization of the transcription termination factor from human mitochondria". J. Biol. Chem. 268 (11): 8123–30. doi:10.1016/S0021-9258(18)53070-2. PMID 7681833. Arhivirano s originala, 17. 4. 2020. Pristupljeno 27. 9. 2021.
- ^ Asin-Cayuela J, Helm M, Attardi G (april 2004). "A monomer-to-trimer transition of the human mitochondrial transcription termination factor (mTERF) is associated with a loss of in vitro activity". J. Biol. Chem. 279 (15): 15670–7. doi:10.1074/jbc.M312537200. PMID 14744862.
- ^ Asin-Cayuela J, Schwend T, Farge G, Gustafsson CM (juli 2005). "The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form". J. Biol. Chem. 280 (27): 25499–505. doi:10.1074/jbc.M501145200. PMID 15899902.
- ^ "UniProt, Q99551" (jezik: engleski). Pristupljeno 27. 9. 2021.
Dopunska literatura
uredi- Daga A, Micol V, Hess D, et al. (1993). "Molecular characterization of the transcription termination factor from human mitochondria". J. Biol. Chem. 268 (11): 8123–30. doi:10.1016/S0021-9258(18)53070-2. PMID 7681833.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Fernandez-Silva P, Martinez-Azorin F, Micol V, Attardi G (1997). "The human mitochondrial transcription termination factor (mTERF) is a multizipper protein but binds to DNA as a monomer, with evidence pointing to intramolecular leucine zipper interactions". EMBO J. 16 (5): 1066–79. doi:10.1093/emboj/16.5.1066. PMC 1169706. PMID 9118945.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Sanger Centre, The; Washington University Genome Sequencing Cente, The (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi:10.1101/gr.8.11.1097. PMID 9847074.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology". Science. 300 (5620): 767–72. Bibcode:2003Sci...300..767S. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205.
- Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
- Asin-Cayuela J, Helm M, Attardi G (2004). "A monomer-to-trimer transition of the human mitochondrial transcription termination factor (mTERF) is associated with a loss of in vitro activity". J. Biol. Chem. 279 (15): 15670–7. doi:10.1074/jbc.M312537200. PMID 14744862.
- Prieto-Martín A, Montoya J, Martínez-Azorín F (2004). "Phosphorylation of rat mitochondrial transcription termination factor (mTERF) is required for transcription termination but not for binding to DNA". Nucleic Acids Res. 32 (7): 2059–68. doi:10.1093/nar/gkh528. PMC 407814. PMID 15087485.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Asin-Cayuela J, Schwend T, Farge G, Gustafsson CM (2005). "The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form". J. Biol. Chem. 280 (27): 25499–505. doi:10.1074/jbc.M501145200. PMID 15899902.
- Hyvärinen AK, Pohjoismäki JL, Reyes A, et al. (2007). "The mitochondrial transcription termination factor mTERF modulates replication pausing in human mitochondrial DNA". Nucleic Acids Res. 35 (19): 6458–74. doi:10.1093/nar/gkm676. PMC 2095818. PMID 17884915.