4fjo
From Proteopedia
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{{STRUCTURE_4fjo| PDB=4fjo | SCENE= }} | {{STRUCTURE_4fjo| PDB=4fjo | SCENE= }} | ||
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===Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex=== | ===Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex=== | ||
| + | {{ABSTRACT_PUBMED_22859295}} | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/DPOLZ_MOUSE DPOLZ_MOUSE]] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis (By similarity). [[http://www.uniprot.org/uniprot/REV1_MOUSE REV1_MOUSE]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:11711549</ref> [[http://www.uniprot.org/uniprot/MD2L2_MOUSE MD2L2_MOUSE]] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (By similarity). [[http://www.uniprot.org/uniprot/POLK_MOUSE POLK_MOUSE]] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).<ref>PMID:12432099</ref> | ||
==About this Structure== | ==About this Structure== | ||
[[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. | [[4fjo]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJO OCA]. | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:022859295</ref><references group="xtra"/><references/> | ||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
Revision as of 09:45, 19 June 2013
Contents |
Structure of the Rev1 CTD-Rev3/7-Pol kappa RIR complex
Template:ABSTRACT PUBMED 22859295
Function
[DPOLZ_MOUSE] Interacts with MAD2L2 to form the error prone DNA polymerase zeta involved in translesion DNA synthesis (By similarity). [REV1_MOUSE] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.[1] [MD2L2_MOUSE] Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (By similarity). [POLK_MOUSE] DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).[2]
About this Structure
4fjo is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Wojtaszek J, Lee CJ, D'Souza S, Minesinger B, Kim H, D'Andrea AD, Walker GC, Zhou P. Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev1, heterodimeric polymerase (Pol) zeta, and Pol kappa. J Biol Chem. 2012 Sep 28;287(40):33836-46. Epub 2012 Aug 2. PMID:22859295 doi:10.1074/jbc.M112.394841
- ↑ Masuda Y, Takahashi M, Fukuda S, Sumii M, Kamiya K. Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein. J Biol Chem. 2002 Jan 25;277(4):3040-6. Epub 2001 Nov 15. PMID:11711549 doi:10.1074/jbc.M110149200
- ↑ Ogi T, Shinkai Y, Tanaka K, Ohmori H. Polkappa protects mammalian cells against the lethal and mutagenic effects of benzo[a]pyrene. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15548-53. Epub 2002 Nov 13. PMID:12432099 doi:10.1073/pnas.222377899
