POLRMT
{{Short description|Protein-coding gene in the species Homo sapiens}}
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DNA-directed RNA polymerase, mitochondrial is an enzyme that in humans is encoded by the POLRMT gene.{{cite journal | vauthors = Tiranti V, Savoia A, Forti F, D'Apolito MF, Centra M, Rocchi M, Zeviani M | title = Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database | journal = Human Molecular Genetics | volume = 6 | issue = 4 | pages = 615–625 | date = April 1997 | pmid = 9097968 | doi = 10.1093/hmg/6.4.615 | doi-access = free }}{{cite web | title = Entrez Gene: POLRMT polymerase (RNA) mitochondrial (DNA directed)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5442}}
Function
This gene encodes a mitochondrial DNA-directed RNA polymerase. The gene product is responsible for mitochondrial gene expression as well as for providing RNA primers for initiation of replication of the mitochondrial genome. Although this polypeptide has the same function as the three nuclear DNA-directed RNA polymerases, it is more closely related to RNA polymerases of bacteriophage (including T7 RNA polymerase), mitochondrial polymerases of lower eukaryotes as well as chloroplastic RpoT polymerases.
Structure
The structure of the enzyme has been solved. It exhibits an overall structure similar to that of phage RNAP, but the initiation mechanism is different in that it requires initiation factors TFAM (only in mammals) and TFB2M.{{cite journal | vauthors = Hillen HS, Morozov YI, Sarfallah A, Temiakov D, Cramer P | title = Structural Basis of Mitochondrial Transcription Initiation | journal = Cell | volume = 171 | issue = 5 | pages = 1072–1081.e10 | date = November 2017 | pmid = 29149603 | pmc = 6590061 | doi = 10.1016/j.cell.2017.10.036 }} Elongation requires the elongation factor TEFM.{{cite journal | vauthors = Hillen HS, Parshin AV, Agaronyan K, Morozov YI, Graber JJ, Chernev A, Schwinghammer K, Urlaub H, Anikin M, Cramer P, Temiakov D | title = Mechanism of Transcription Anti-termination in Human Mitochondria | journal = Cell | volume = 171 | issue = 5 | pages = 1082–1093.e13 | date = November 2017 | pmid = 29033127 | pmc = 5798601 | doi = 10.1016/j.cell.2017.09.035 }} The exact termination process is less understood, but MTERF1 is thought to play a role.{{cite journal | vauthors = D'Souza AR, Minczuk M | title = Mitochondrial transcription and translation: overview | journal = Essays in Biochemistry | volume = 62 | issue = 3 | pages = 309–320 | date = July 2018 | pmid = 30030363 | pmc = 6056719 | doi = 10.1042/EBC20170102 }}
References
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Further reading
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- {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–174 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
- {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–156 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
- {{cite journal | vauthors = Falkenberg M, Gaspari M, Rantanen A, Trifunovic A, Larsson NG, Gustafsson CM | title = Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA | journal = Nature Genetics | volume = 31 | issue = 3 | pages = 289–294 | date = July 2002 | pmid = 12068295 | doi = 10.1038/ng909 | s2cid = 11164308 | author-link1 = Maria Falkenberg }}
- {{cite journal | vauthors = McCulloch V, Shadel GS | title = Human mitochondrial transcription factor B1 interacts with the C-terminal activation region of h-mtTFA and stimulates transcription independently of its RNA methyltransferase activity | journal = Molecular and Cellular Biology | volume = 23 | issue = 16 | pages = 5816–5824 | date = August 2003 | pmid = 12897151 | pmc = 166325 | doi = 10.1128/MCB.23.16.5816-5824.2003 }}
- {{cite journal | vauthors = Graziewicz MA, Longley MJ, Bienstock RJ, Zeviani M, Copeland WC | title = Structure-function defects of human mitochondrial DNA polymerase in autosomal dominant progressive external ophthalmoplegia | journal = Nature Structural & Molecular Biology | volume = 11 | issue = 8 | pages = 770–776 | date = August 2004 | pmid = 15258572 | doi = 10.1038/nsmb805 | s2cid = 12460199 }}
- {{cite journal | vauthors = Gaspari M, Falkenberg M, Larsson NG, Gustafsson CM | title = The mitochondrial RNA polymerase contributes critically to promoter specificity in mammalian cells | journal = The EMBO Journal | volume = 23 | issue = 23 | pages = 4606–4614 | date = November 2004 | pmid = 15526033 | pmc = 533051 | doi = 10.1038/sj.emboj.7600465 }}
- {{cite journal | vauthors = Kravchenko JE, Rogozin IB, Koonin EV, Chumakov PM | title = Transcription of mammalian messenger RNAs by a nuclear RNA polymerase of mitochondrial origin | journal = Nature | volume = 436 | issue = 7051 | pages = 735–739 | date = August 2005 | pmid = 16079853 | pmc = 1352165 | doi = 10.1038/nature03848 | bibcode = 2005Natur.436..735K }}
- {{cite journal | vauthors = Wang Z, Cotney J, Shadel GS | title = Human mitochondrial ribosomal protein MRPL12 interacts directly with mitochondrial RNA polymerase to modulate mitochondrial gene expression | journal = The Journal of Biological Chemistry | volume = 282 | issue = 17 | pages = 12610–12618 | date = April 2007 | pmid = 17337445 | pmc = 2606046 | doi = 10.1074/jbc.M700461200 | doi-access = free }}
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External links
- {{PDBe-KB2|O00411|Human DNA-directed RNA polymerase, mitochondrial (POLRMT)}}
{{Kinases}}
{{Enzymes}}
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