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{{Infobox_gene}}
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'''Mitochondrial transcription termination factor''', also known as '''MTERF''', is a [[protein]] which in humans is encoded by the ''MTERF'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MTERF mitochondrial transcription termination factor| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7978| accessdate = }}</ref><ref name="pmid7681833">{{cite journal |vauthors=Daga A, Micol V, Hess D, Aebersold R, Attardi G | title = Molecular characterization of the transcription termination factor from human mitochondria | journal = J. Biol. Chem. | volume = 268 | issue = 11 | pages = 8123–30 |date=April 1993 | pmid = 7681833 | doi = | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=7681833 | issn = }}</ref><ref name="pmid14744862">{{cite journal |vauthors=Asin-Cayuela J, Helm M, Attardi G | title = A monomer-to-trimer transition of the human mitochondrial transcription termination factor (mTERF) is associated with a loss of in vitro activity | journal = J. Biol. Chem. | volume = 279 | issue = 15 | pages = 15670–7 |date=April 2004 | pmid = 14744862 | doi = 10.1074/jbc.M312537200 | url = | issn = }}</ref><ref name="pmid15899902">{{cite journal |vauthors=Asin-Cayuela J, Schwend T, Farge G, Gustafsson CM | title = The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form | journal = J. Biol. Chem. | volume = 280 | issue = 27 | pages = 25499–505 |date=July 2005 | pmid = 15899902 | doi = 10.1074/jbc.M501145200 | url = | issn = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a [[mitochondrion|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 [[transfer RNA|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.<ref name="entrez"/>
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Mitochondrial transcription termination factor
| HGNCid = 21463
| Symbol = MTERF
| AltSymbols =; MGC131634
| OMIM = 602318
| ECnumber = 
| Homologene = 5073
| MGIid = 1918240
| GeneAtlas_image1 = PBB_GE_MTERF_204871_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003690 |text = double-stranded DNA binding}} {{GNF_GO|id=GO:0003715 |text = transcription termination factor activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006393 |text = RNA transcription termination from mitochondrial promoter}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7978
    | Hs_Ensembl = ENSG00000127989
    | Hs_RefseqProtein = NP_008911
    | Hs_RefseqmRNA = NM_006980
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 91339957
    | Hs_GenLoc_end = 91347952
    | Hs_Uniprot = Q99551
    | Mm_EntrezGene = 208595
    | Mm_Ensembl = ENSMUSG00000053178
    | Mm_RefseqmRNA = NM_001042670
    | Mm_RefseqProtein = NP_001036135
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 4198373
    | Mm_GenLoc_end = 4203657
    | Mm_Uniprot = Q8CHZ9
  }}
}}
'''Mitochondrial transcription termination factor''', also known as '''MTERF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MTERF mitochondrial transcription termination factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7978| accessdate = }}</ref>


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==References==
{{PBB_Summary
{{reflist}}
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: MTERF mitochondrial transcription termination factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7978| accessdate = }}</ref>
}}


==References==
{{reflist|2}}
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Daga A, Micol V, Hess D, ''et al.'' |title=Molecular characterization of the transcription termination factor from human mitochondria. |journal=J. Biol. Chem. |volume=268 |issue= 11 |pages= 8123-30 |year= 1993 |pmid= 7681833 |doi=  }}
*{{cite journal   |vauthors=Daga A, Micol V, Hess D, etal |title=Molecular characterization of the transcription termination factor from human mitochondria. |journal=J. Biol. Chem. |volume=268 |issue= 11 |pages= 8123–30 |year= 1993 |pmid= 7681833 |doi=  }}
*{{cite journal  | author=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= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{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= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Fernandez-Silva P, Martinez-Azorin F, Micol V, Attardi G |title=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. |journal=EMBO J. |volume=16 |issue= 5 |pages= 1066-79 |year= 1997 |pmid= 9118945 |doi= 10.1093/emboj/16.5.1066 }}
*{{cite journal  |vauthors=Fernandez-Silva P, Martinez-Azorin F, Micol V, Attardi G |title=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. |journal=EMBO J. |volume=16 |issue= 5 |pages= 1066–79 |year= 1997 |pmid= 9118945 |doi= 10.1093/emboj/16.5.1066 | pmc=1169706 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal  | author= |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097-108 |year= 1999 |pmid= 9847074 |doi=  }}
*{{cite journal  |title=Toward a complete human genome sequence. |journal=Genome Res. |volume=8 |issue= 11 |pages= 1097–108 |year= 1999 |pmid= 9847074 |doi=  10.1101/gr.8.11.1097}}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Scherer SW, Cheung J, MacDonald JR, ''et al.'' |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767-72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423 }}
*{{cite journal   |vauthors=Scherer SW, Cheung J, MacDonald JR, etal |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767–72 |year= 2003 |pmid= 12690205 | pmc=2882961 |doi= 10.1126/science.1083423 }}
*{{cite journal | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal   |vauthors=Hillier LW, Fulton RS, Fulton LA, etal |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157–64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal  | author=Asin-Cayuela J, Helm M, Attardi G |title=A monomer-to-trimer transition of the human mitochondrial transcription termination factor (mTERF) is associated with a loss of in vitro activity. |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 15670-7 |year= 2004 |pmid= 14744862 |doi= 10.1074/jbc.M312537200 }}
*{{cite journal  |vauthors=Asin-Cayuela J, Helm M, Attardi G |title=A monomer-to-trimer transition of the human mitochondrial transcription termination factor (mTERF) is associated with a loss of in vitro activity. |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 15670–7 |year= 2004 |pmid= 14744862 |doi= 10.1074/jbc.M312537200 }}
*{{cite journal  | author=Prieto-Martín A, Montoya J, Martínez-Azorín F |title=Phosphorylation of rat mitochondrial transcription termination factor (mTERF) is required for transcription termination but not for binding to DNA. |journal=Nucleic Acids Res. |volume=32 |issue= 7 |pages= 2059-68 |year= 2004 |pmid= 15087485 |doi= 10.1093/nar/gkh528 }}
*{{cite journal  |vauthors=Prieto-Martín A, Montoya J, Martínez-Azorín F |title=Phosphorylation of rat mitochondrial transcription termination factor (mTERF) is required for transcription termination but not for binding to DNA. |journal=Nucleic Acids Res. |volume=32 |issue= 7 |pages= 2059–68 |year= 2004 |pmid= 15087485 |doi= 10.1093/nar/gkh528 | pmc=407814 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal  | author=Asin-Cayuela J, Schwend T, Farge G, Gustafsson CM |title=The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form. |journal=J. Biol. Chem. |volume=280 |issue= 27 |pages= 25499-505 |year= 2005 |pmid= 15899902 |doi= 10.1074/jbc.M501145200 }}
*{{cite journal  |vauthors=Asin-Cayuela J, Schwend T, Farge G, Gustafsson CM |title=The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form. |journal=J. Biol. Chem. |volume=280 |issue= 27 |pages= 25499–505 |year= 2005 |pmid= 15899902 |doi= 10.1074/jbc.M501145200 }}
*{{cite journal | author=Hyvärinen AK, Pohjoismäki JL, Reyes A, ''et al.'' |title=The mitochondrial transcription termination factor mTERF modulates replication pausing in human mitochondrial DNA. |journal=Nucleic Acids Res. |volume=35 |issue= 19 |pages= 6458-74 |year= 2007 |pmid= 17884915 |doi= 10.1093/nar/gkm676 }}
*{{cite journal   |vauthors=Hyvärinen AK, Pohjoismäki JL, Reyes A, etal |title=The mitochondrial transcription termination factor mTERF modulates replication pausing in human mitochondrial DNA. |journal=Nucleic Acids Res. |volume=35 |issue= 19 |pages= 6458–74 |year= 2007 |pmid= 17884915 |doi= 10.1093/nar/gkm676 | pmc=2095818 }}
}}
}}
{{refend}}
{{refend}}


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Revision as of 07:01, 4 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Mitochondrial transcription termination factor, also known as MTERF, is a protein which in humans is encoded by the MTERF gene.[1][2][3][4]

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.[1]

References

  1. 1.0 1.1 "Entrez Gene: MTERF mitochondrial transcription termination factor".
  2. 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. PMID 7681833.
  3. 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.
  4. 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.

Further reading