MTERF1

MTERF1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3MVA, 3MVB, 3N6S, 3N7Q, 5CO0, 5CRJ, 5CKY, 5CRK
Identifiers
Aliases	MTERF1 , MTERF, mitochondrial transcription termination factor 1
External IDs	OMIM: 602318 MGI: 3704243 HomoloGene: 5073 GeneCards: MTERF1
Gene location (Human)
Chr.	Chromosome 7 (human)
End	91,880,702 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	4,247,651 bp
RNA expression pattern
	Top expressed in
	corpus callosum; ; Achilles tendon; ; lymph node; ; endometrium; ; islet of Langerhans; ; monocyte; ; ganglionic eminence; ; rectum; ; smooth muscle tissue; ; appendix;
	Top expressed in
	secondary oocyte; ; bone marrow; ; morula; ; pancreas; ; thymus; ; white adipose tissue; ; adrenal gland; ; quadriceps femoris muscle; ; urinary bladder; ; islet of Langerhans;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	DNA binding ; protein binding ; double-stranded DNA binding ; RNA binding ;
Cellular component	mitochondrial matrix ; mitochondrial nucleoid ; mitochondrion ; cytosol ;
Biological process	termination of mitochondrial transcription ; mitochondrion organization ; regulation of transcription, DNA-templated ; transcription, DNA-templated ; DNA geometric change ; DNA-templated transcription, termination ;
	Sources:Amigo / QuickGO
Orthologs
	7978
	208595
	ENSG00000127989
	ENSMUSG00000053178
	Q99551
	B9EJ57
	NM_001301134 ; NM_001301135 ; NM_006980
	NM_001042670
	NP_001288063 ; NP_001288064 ; NP_008911
	NP_001036135
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

Mitochondrial transcription termination factor 1, also known as MTERF1, is a protein which in humans is encoded by the MTERF gene.^[5]^[6]^[7]^[8]

This gene encodes a mitochondrial transcription termination factor. This protein participates in attenuating transcription from the mitochondrial genome; this attenuation allows higher levels of expression of 16S ribosomal RNA relative to the tRNA gene downstream. The product of this gene has three leucine zipper motifs bracketed by two basic domains that are all required for DNA binding. There is evidence that, for this protein, the zippers participate in intramolecular interactions that establish the three-dimensional structure required for DNA binding.^[5]

Related Research Articles

Nuclear respiratory factor 1, also known as Nrf1, Nrf-1, NRF1 and NRF-1, encodes a protein that homodimerizes and functions as a transcription factor which activates the expression of some key metabolic genes regulating cellular growth and nuclear genes required for respiration, heme biosynthesis, and mitochondrial DNA transcription and replication. The protein has also been associated with the regulation of neurite outgrowth. Alternate transcriptional splice variants, which encode the same protein, have been characterized. Additional variants encoding different protein isoforms have been described but they have not been fully characterized. Confusion has occurred in bibliographic databases due to the shared symbol of NRF1 for this gene and for "nuclear factor -like 1" which has an official symbol of NFE2L1.

Cyclic AMP-dependent transcription factor ATF-1 is a protein that in humans is encoded by the ATF1 gene.

Activating transcription factor 6, also known as ATF6, is a protein that, in humans, is encoded by the ATF6 gene and is involved in the unfolded protein response.

Activating transcription factor 2, also known as ATF2, is a protein that, in humans, is encoded by the ATF2 gene.

Cux1 is a homeodomain protein that in humans is encoded by the CUX1 gene.

DNA-binding protein inhibitor ID-3 is a protein that in humans is encoded by the ID3 gene.

Calcium/calmodulin-dependent protein kinase type 1 is an enzyme that in humans is encoded by the CAMK1 gene.

Interferon regulatory factor 9 is a protein that in humans is encoded by the IRF9 gene, previously known as ISGF3G.

Nuclear transcription factor Y subunit gamma is a protein that in humans is encoded by the NFYC gene.

Krueppel-like factor 10 is a protein that in humans is encoded by the KLF10 gene.

Zinc finger and BTB domain-containing protein 7A is a protein that in humans is encoded by the ZBTB7A gene.

Heat shock protein 75 kDa, mitochondrial is a protein that in humans is encoded by the TRAP1 gene.

Transcription factor TFIIIB component B″ homolog also known as TFIIIB150 is a protein that in humans is encoded by the BDP1 gene.

Helicase SRCAP is an enzyme that in humans is encoded by the SRCAP gene.

Peroxisome proliferator-activated receptor gamma coactivator-related protein 1 is a protein that in humans is encoded by the PPRC1 gene.

28S ribosomal protein S22, mitochondrial is a protein that in humans is encoded by the MRPS22 gene.

Zinc finger protein 143 is a protein that in humans is encoded by the ZNF143 gene.

POLRMT is a symbol of RNA polymerase mitochondrial

Upstream-binding protein 1 is a protein that in humans is encoded by the UBP1 gene.

Chloride channel CLIC-like 1 also known as CLCC1 is a human gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000127989 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000053178 - Ensembl, May 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.
1 2 "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.
↑ 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 (July 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.

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. Bibcode:2002PNAS...9916899M. 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.

This article on a gene on human chromosome 7 is a stub. You can help Wikipedia by expanding it.

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000127989 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000053178 - 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.

[entrez-5] 1 2 "Entrez Gene: MTERF mitochondrial transcription termination factor".

[pmid7681833-6] 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.

[pmid14744862-7] 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.

[pmid15899902-8] Asin-Cayuela J, Schwend T, Farge G, Gustafsson CM (July 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.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

MTERF1

Related Research Articles

References

Further reading