POLRMT

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3SPA, 4BOC

Identifiers

Aliases

POLRMT, APOLMT, MTRNAP, MTRPOL, h-mtRPOL, polymerase (RNA) mitochondrial

External IDs

MGI: 1915843 HomoloGene: 37996 GeneCards: POLRMT

Gene ontology
Molecular function	• DNA-directed 5'-3' RNA polymerase activity • transferase activity • DNA binding • nucleotidyltransferase activity • poly(A) RNA binding • protein binding
Cellular component	• mitochondrial matrix • mitochondrial nucleoid • mitochondrion
Biological process	• transcription from mitochondrial promoter • transcription initiation from mitochondrial promoter • mitochondrion organization • transcription, DNA-templated
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


5442


216151

Ensembl


ENSG00000099821


ENSMUSG00000020329

UniProt


O00411


Q8BKF1

RefSeq (mRNA)


NM_005035


NM_172551

RefSeq (protein)


NP_005026.3


NP_766139.2

Location (UCSC)

Chr 19: 0.62 – 0.63 Mb

Chr 10: 79.74 – 79.75 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

DNA-directed RNA polymerase, mitochondrial is an enzyme that in humans is encoded by the POLRMT gene.^[3]^[4]

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 and mitochondrial polymerases of lower eukaryotes.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Tiranti V, Savoia A, Forti F, D'Apolito MF, Centra M, Rocchi M, Zeviani M (Jul 1997). "Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database". Hum Mol Genet. 6 (4): 615–25. doi:10.1093/hmg/6.4.615. PMID 9097968.
1 2 "Entrez Gene: POLRMT polymerase (RNA) mitochondrial (DNA directed)".

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.
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.
Falkenberg M, Gaspari M, Rantanen A, et al. (2002). "Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA". Nat. Genet. 31 (3): 289–94. doi:10.1038/ng909. PMID 12068295.
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.
McCulloch V, Shadel GS (2003). "Human mitochondrial transcription factor B1 interacts with the C-terminal activation region of h-mtTFA and stimulates transcription independently of its RNA methyltransferase activity". Mol. Cell. Biol. 23 (16): 5816–24. doi:10.1128/MCB.23.16.5816-5824.2003. PMC 166325. PMID 12897151.
Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature. 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.
Graziewicz MA, Longley MJ, Bienstock RJ, et al. (2004). "Structure-function defects of human mitochondrial DNA polymerase in autosomal dominant progressive external ophthalmoplegia". Nat. Struct. Mol. Biol. 11 (8): 770–6. doi:10.1038/nsmb805. PMID 15258572.
Gaspari M, Falkenberg M, Larsson NG, Gustafsson CM (2005). "The mitochondrial RNA polymerase contributes critically to promoter specificity in mammalian cells". EMBO J. 23 (23): 4606–14. doi:10.1038/sj.emboj.7600465. PMC 533051. PMID 15526033.
Kravchenko JE, Rogozin IB, Koonin EV, Chumakov PM (2005). "Transcription of mammalian messenger RNAs by a nuclear RNA polymerase of mitochondrial origin". Nature. 436 (7051): 735–9. doi:10.1038/nature03848. PMC 1352165. PMID 16079853.
Wang Z, Cotney J, Shadel GS (2007). "Human mitochondrial ribosomal protein MRPL12 interacts directly with mitochondrial RNA polymerase to modulate mitochondrial gene expression". J. Biol. Chem. 282 (17): 12610–8. doi:10.1074/jbc.M700461200. PMC 2606046. PMID 17337445.

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase

2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase

2.7.3: N acceptor	Creatine

2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
(P₂O₇)

2.7.7: nucleotidyltransferase
(PO₄-nucleoside)

Polymerase

DNA polymerase	DNA-directed DNA polymerase I II III IV V RNA-directed DNA polymerase Reverse transcriptase Telomerase DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase

RNA nucleotidyltransferase	RNA polymerase/DNA-directed RNA polymerase RNA polymerase I RNA polymerase II RNA polymerase III RNA polymerase IV Primase RNA-dependent RNA polymerase PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase

Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases

2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases

2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases

2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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POLRMT

Function

References

Further reading