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rdf:type |
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lifeskim:mentions |
umls-concept:C0012940,
umls-concept:C0043393,
umls-concept:C0084913,
umls-concept:C0376525,
umls-concept:C1425416,
umls-concept:C1514562,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
8
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pubmed:dateCreated |
1997-8-25
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pubmed:abstractText |
The RAD6 gene of Saccharomyces cerevisiae encodes a ubiquitin-conjugating enzyme required for postreplicational repair of UV-damaged DNA and for damage-induced mutagenesis. In addition, Rad6 functions in the N end rule pathway of protein degradation. Rad6 mediates its DNA repair role via its association with Rad18, whose DNA binding activity may target the Rad6-Rad18 complex to damaged sites in DNA. In its role in N end-dependent protein degradation, Rad6 interacts with the UBR1-encoded ubiquitin protein ligase (E3) enzyme. Previous studies have indicated the involvement of N-terminal and C-terminal regions of Rad6 in interactions with Ubr1. Here, we identify the regions of Rad6 and Rad18 that are involved in the dimerization of these two proteins. We show that a region of 40 amino acids towards the C terminus of Rad18 (residues 371 to 410) is sufficient for interaction with Rad6. This region of Rad18 contains a number of nonpolar residues that have been conserved in helix-loop-helix motifs of other proteins. Our studies indicate the requirement for residues 141 to 149 at the C terminus, and suggest the involvement of residues 10 to 22 at the N terminus of Rad6, in the interaction with Rad18. Each of these regions of Rad6 is indicated to form an amphipathic helix.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-1310896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-1321826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-1651502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-1690605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-1717990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-1902572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-2052013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-2065660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-2154679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-2184030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-2850263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-2970061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-3285176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-3306404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-3881753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-4376097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-7038396,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-7526205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-770231,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-7729428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-7926769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-8126734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-8263911,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-8384143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-8436296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-8505328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-8790390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9234711-8898388
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4536-43
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9234711-Amino Acid Sequence,
pubmed-meshheading:9234711-DNA Repair,
pubmed-meshheading:9234711-DNA-Binding Proteins,
pubmed-meshheading:9234711-Dimerization,
pubmed-meshheading:9234711-Helix-Loop-Helix Motifs,
pubmed-meshheading:9234711-Ligases,
pubmed-meshheading:9234711-Molecular Sequence Data,
pubmed-meshheading:9234711-Protein Structure, Secondary,
pubmed-meshheading:9234711-Recombinant Fusion Proteins,
pubmed-meshheading:9234711-Saccharomyces cerevisiae,
pubmed-meshheading:9234711-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9234711-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:9234711-Zinc Fingers
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pubmed:year |
1997
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pubmed:articleTitle |
Domains required for dimerization of yeast Rad6 ubiquitin-conjugating enzyme and Rad18 DNA binding protein.
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pubmed:affiliation |
Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston 77555-1061, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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