REV1: Difference between revisions
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{{PBB_Summary |
{{PBB_Summary |
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| summary_text = This gene encodes a protein with similarity to the S. cerevisiae mutagenesis protein Rev1. The Rev1 proteins contain a BRCT domain, which is important in protein-protein interactions. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.<ref name="entrez"/> |
| summary_text = This gene encodes a protein with similarity to the [[S. cerevisiae]] [[mutagenesis]] protein Rev1. The Rev1 proteins contain a [[BRCT domain]], which is important in [[protein-protein interactions]]. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA [[polymerase | polymerases]] involved in [[translesion synthesis]] (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.<ref name="entrez"/> |
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}} Rev1 is a [[DNA polymerase#Family Y|Y family DNA polymerase]]; it is sometimes referred to as a ''deoxycytidyl transferase'' because it only inserts [[deoxycytidine]] (dC) across from lesions. Whether [[Guanine|G]], [[Adenine|A]], [[Thymine|T]], [[Cytidine|C]], or an [[AP site|abasic site]], Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an [[arginine]] as a template which complements well with C.<ref>{{Cite journal|url = http://www.ncbi.nlm.nih.gov/pubmed/16195463|title = Rev1 employs a novel mechanism of DNA synthesis using a protein template|last = Nair|first = DT|date = Sep 30, 2005|journal = Science|doi = 10.1126/science.1116336|pmid = 16195463|access-date = Feb 6, 2015}}</ref> Yet it is believed{{By whom|date=May 2011}} that Rev1 rarely uses its polymerase activity |
}} Rev1 is a [[DNA polymerase#Family Y|Y family DNA polymerase]]; it is sometimes referred to as a ''deoxycytidyl transferase'' because it only inserts [[deoxycytidine]] (dC) across from lesions. Whether [[Guanine|G]], [[Adenine|A]], [[Thymine|T]], [[Cytidine|C]], or an [[AP site|abasic site]], Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an [[arginine]] as a template which complements well with C.<ref>{{Cite journal|url = http://www.ncbi.nlm.nih.gov/pubmed/16195463|title = Rev1 employs a novel mechanism of DNA synthesis using a protein template|last = Nair|first = DT|date = Sep 30, 2005|journal = Science|doi = 10.1126/science.1116336|pmid = 16195463|access-date = Feb 6, 2015}}</ref> Yet it is believed{{By whom|date=May 2011}} that Rev1 rarely uses its polymerase activity; rather it is thought that Rev1's primary role is as a protein landing pad, whereby it helps direct the recruitment of TLS proteins, especially Pol ζ ([[REV3L|Rev3]]/Rev7). |
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==Interactions== |
==Interactions== |
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REV1 has been shown to [[Protein-protein interaction|interact]] with [[MAD2L2]].<ref name=pmid11485998>{{cite journal |last=Murakumo |first=Y |authorlink= |author2=Ogura Y |author3=Ishii H |author4=Numata S |author5=Ichihara M |author6=Croce C M |author7=Fishel R |author8=Takahashi M |date=September 2001 |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7 |journal=J. Biol. Chem. |volume=276 |issue=38 |pages=35644–51 |publisher= |location = United States| issn = 0021-9258| pmid = 11485998 |doi = 10.1074/jbc.M102051200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> It is believed that Rev1 may interact with PCNA, once ubiquitylated due to a lesion, and help recruit Pol ζ ([[REV3L|Rev3]]/Rev7) a B family polymerase involved in TLS. |
REV1 has been shown to [[Protein-protein interaction|interact]] with [[MAD2L2]].<ref name=pmid11485998>{{cite journal |last=Murakumo |first=Y |authorlink= |author2=Ogura Y |author3=Ishii H |author4=Numata S |author5=Ichihara M |author6=Croce C M |author7=Fishel R |author8=Takahashi M |date=September 2001 |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7 |journal=J. Biol. Chem. |volume=276 |issue=38 |pages=35644–51 |publisher= |location = United States| issn = 0021-9258| pmid = 11485998 |doi = 10.1074/jbc.M102051200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> It is believed that Rev1 may interact with PCNA, once [[ubiquitylated]] due to a lesion, and help recruit Pol ζ ([[REV3L|Rev3]]/Rev7) a B family polymerase involved in TLS. |
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==References== |
==References== |
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Revision as of 22:28, 25 October 2016
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| Aliases | REV1, REV1L, AIBP80, DNA directed polymerase, REV1 DNA directed polymerase | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 606134; MGI: 1929074; HomoloGene: 32309; GeneCards: REV1; OMA:REV1 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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DNA repair protein REV1 is a protein that in humans is encoded by the REV1 gene.[5][6] Template:PBB Summary Rev1 is a Y family DNA polymerase; it is sometimes referred to as a deoxycytidyl transferase because it only inserts deoxycytidine (dC) across from lesions. Whether G, A, T, C, or an abasic site, Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an arginine as a template which complements well with C.[7] Yet it is believed[by whom?] that Rev1 rarely uses its polymerase activity; rather it is thought that Rev1's primary role is as a protein landing pad, whereby it helps direct the recruitment of TLS proteins, especially Pol ζ (Rev3/Rev7).
Interactions
REV1 has been shown to interact with MAD2L2.[8] It is believed that Rev1 may interact with PCNA, once ubiquitylated due to a lesion, and help recruit Pol ζ (Rev3/Rev7) a B family polymerase involved in TLS.
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000135945 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026082 – 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.
- ^ Lin W, Xin H, Zhang Y, Wu X, Yuan F, Wang Z (Dec 1999). "The human REV1 gene codes for a DNA template-dependent dCMP transferase". Nucleic Acids Res. 27 (22): 4468–75. doi:10.1093/nar/27.22.4468. PMC 148731. PMID 10536157.
- ^ "Entrez Gene: REV1 REV1 homolog (S. cerevisiae)".
- ^ Nair, DT (Sep 30, 2005). "Rev1 employs a novel mechanism of DNA synthesis using a protein template". Science. doi:10.1126/science.1116336. PMID 16195463. Retrieved Feb 6, 2015.
- ^ Murakumo, Y; Ogura Y; Ishii H; Numata S; Ichihara M; Croce C M; Fishel R; Takahashi M (September 2001). "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7". J. Biol. Chem. 276 (38). United States: 35644–51. doi:10.1074/jbc.M102051200. ISSN 0021-9258. PMID 11485998.
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Further reading
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