POLRMT

Protein-coding gene in the species Homo sapiens
POLRMT
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3SPA, 4BOC

Identifiers
AliasesPOLRMT, APOLMT, MTRNAP, MTRPOL, h-mtRPOL, polymerase (RNA) mitochondrial, RNA polymerase mitochondrial, COXPD55
External IDsOMIM: 601778; MGI: 1915843; HomoloGene: 37996; GeneCards: POLRMT; OMA:POLRMT - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for POLRMT
Genomic location for POLRMT
Band19p13.3Start617,221 bp[1]
End633,537 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for POLRMT
Genomic location for POLRMT
Band10|10 C1Start79,571,957 bp[2]
End79,582,415 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • left testis

  • right testis

  • apex of heart

  • testicle

  • mucosa of transverse colon

  • gonad

  • muscle of thigh

  • right lobe of liver

  • gastrocnemius muscle

  • anterior pituitary
Top expressed in
  • right ventricle

  • internal carotid artery

  • external carotid artery

  • temporal muscle

  • primary oocyte

  • sternocleidomastoid muscle

  • triceps brachii muscle

  • muscle of thigh

  • motor neuron

  • digastric muscle
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • DNA-directed 5'-3' RNA polymerase activity
  • transferase activity
  • DNA binding
  • nucleotidyltransferase activity
  • protein binding
  • RNA binding
  • mitochondrial promoter sequence-specific DNA binding
  • sequence-specific DNA binding
Cellular component
  • mitochondrial matrix
  • mitochondrial nucleoid
  • mitochondrion
  • mitochondrial DNA-directed RNA polymerase complex
  • protein-containing complex
Biological process
  • mitochondrial transcription
  • transcription initiation from mitochondrial promoter
  • mitochondrion organization
  • transcription, DNA-templated
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5442

216151

Ensembl

ENSG00000099821

ENSMUSG00000020329

UniProt

O00411

Q8BKF1

RefSeq (mRNA)

NM_005035

NM_172551

RefSeq (protein)

NP_005026

NP_766139
NP_001394721
NP_001394722
NP_001394723
NP_001394724

NP_001394725
NP_001394726
NP_001394727
NP_001394728

Location (UCSC)Chr 19: 0.62 – 0.63 MbChr 10: 79.57 – 79.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

DNA-directed RNA polymerase, mitochondrial is an enzyme that in humans is encoded by the POLRMT gene.[5][6]

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.[6]

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.[7] Elongation requires the elongation factor TEFM.[8] The exact termination process is less understood, but MTERF1 is thought to play a role.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000099821 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020329 – Ensembl, May 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. ^ 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.
  6. ^ a b "Entrez Gene: POLRMT polymerase (RNA) mitochondrial (DNA directed)".
  7. ^ Hillen, HS; Morozov, YI; Sarfallah, A; Temiakov, D; Cramer, P (16 November 2017). "Structural Basis of Mitochondrial Transcription Initiation". Cell. 171 (5): 1072–1081.e10. doi:10.1016/j.cell.2017.10.036. PMC 6590061. PMID 29149603.
  8. ^ Hillen, Hauke S.; Parshin, Andrey V.; Agaronyan, Karen; Morozov, Yaroslav I.; Graber, James J.; Chernev, Aleksandar; Schwinghammer, Kathrin; Urlaub, Henning; Anikin, Michael; Cramer, Patrick; Temiakov, Dmitry (November 2017). "Mechanism of Transcription Anti-termination in Human Mitochondria". Cell. 171 (5): 1082–1093.e13. doi:10.1016/j.cell.2017.09.035. PMC 5798601. PMID 29033127.
  9. ^ D'Souza, AR; Minczuk, M (20 July 2018). "Mitochondrial transcription and translation: overview". Essays in Biochemistry. 62 (3): 309–320. doi:10.1042/EBC20170102. PMC 6056719. PMID 30030363.

Further reading

  • 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. S2CID 11164308.
  • 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004Natur.428..529G. 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. S2CID 12460199.
  • 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. Bibcode:2005Natur.436..735K. 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.

External links

  • Overview of all the structural information available in the PDB for UniProt: O00411 (Human DNA-directed RNA polymerase, mitochondrial (POLRMT)) at the PDBe-KB.


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Transferases: phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor
2.7.2: COOH acceptor
2.7.3: N acceptor
2.7.4: PO4 acceptor
2.7.6: diphosphotransferase
(P2O7)2.7.7: nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Phosphorolytic
3' to 5' exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor)
2.7.10: protein-tyrosine
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
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