1t4w: Difference between revisions

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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/CEP1_CAEEL CEP1_CAEEL] Transcriptional activator that binds the same DNA consensus sequence as p53. Has a role in normal development to ensure proper meiotic chromosome segregation. Promotes apoptosis under conditions of cellular and genotoxic stress in response to DNA damage, hypoxia, or starvation. However, not required for DNA repair in response to UV-C or to regulate cell-cycle progression. Required for induction of ced-13 in response to DNA damage. Regulates germline proliferation by activating phg-1.<ref>PMID:11696333</ref> <ref>PMID:11557844</ref> <ref>PMID:12445383</ref> <ref>PMID:15273685</ref> <ref>PMID:15707894</ref> <ref>PMID:15605074</ref> <ref>PMID:16319925</ref> <ref>PMID:17276923</ref> <ref>PMID:17186023</ref> <ref>PMID:17347667</ref> <ref>PMID:17895432</ref> <ref>PMID:18627611</ref> <ref>PMID:18836529</ref> <ref>PMID:19015549</ref>  
[https://www.uniprot.org/uniprot/CEP1_CAEEL CEP1_CAEEL] Transcriptional activator that binds the same DNA consensus sequence as p53. Has a role in normal development to ensure proper meiotic chromosome segregation. Promotes apoptosis under conditions of cellular and genotoxic stress in response to DNA damage, hypoxia, or starvation. However, not required for DNA repair in response to UV-C or to regulate cell-cycle progression. Required for induction of ced-13 in response to DNA damage. Regulates germline proliferation by activating phg-1.<ref>PMID:11696333</ref> <ref>PMID:11557844</ref> <ref>PMID:12445383</ref> <ref>PMID:15273685</ref> <ref>PMID:15707894</ref> <ref>PMID:15605074</ref> <ref>PMID:16319925</ref> <ref>PMID:17276923</ref> <ref>PMID:17186023</ref> <ref>PMID:17347667</ref> <ref>PMID:17895432</ref> <ref>PMID:18627611</ref> <ref>PMID:18836529</ref> <ref>PMID:19015549</ref>  
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== Publication Abstract from PubMed ==
The DNA binding domains of human p53 and Cep-1, its C. elegans ortholog, recognize essentially identical DNA sequences despite poor sequence similarity. We solved the three-dimensional structure of the Cep-1 DNA binding domain in the absence of DNA and compared it to that of human p53. The two domains have similar overall folds. However, three loops, involved in DNA and Zn binding in human p53, contain small alpha helices in Cep-1. The alpha helix in loop L3 of Cep-1 orients the side chains of two conserved arginines toward DNA; in human p53, both arginines are mutation hotspots, but only one contacts DNA. The alpha helix in loop L1 of Cep-1 repositions the entire loop, making it unlikely for residues of this loop to contact bases in the major groove of DNA, as occurs in human p53. Thus, during evolution there have been considerable changes in the structure of the p53 DNA binding domain.
Structural differences in the DNA binding domains of human p53 and its C. elegans ortholog Cep-1.,Huyen Y, Jeffrey PD, Derry WB, Rothman JH, Pavletich NP, Stavridi ES, Halazonetis TD Structure. 2004 Jul;12(7):1237-43. PMID:15242600<ref>PMID:15242600</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
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