Linked Life Data

15530417

Source:http://linkedlifedata.com/resource/pubmed/id/15530417

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-11-8
pubmed:abstractText
The ubiquitin system is a well-conserved and pervasive process for post-synthetic modification of proteins. Three key components of the pathway are required for ubiquitination to occur: the E1 ubiquitin activating enzyme, the E2 ubiquitin conjugating enzyme, and the E3 ubiquitin ligase. There are several different E2 ubiquitin conjugating enzymes and an even greater number of E3 ubiquitin ligases. Interactions between these two groups are critical for substrate ubiquitination. This study reports a two-hybrid analysis of interactions within the ubiquitin system of Caenorhabditis elegans. Forty-three RING finger proteins (presumed E3 ubiquitin ligases) and 14 predicted E2 ubiquitin conjugating enzymes were included in the screen. A total of 31 E2-E3 interactions were uncovered. In addition, the UBC-13 conjugating enzyme was observed to interact with two different E2s, UEV-1 and UBC-1. The interaction of UBC-1 and UBC-13 was confirmed with in vitro ubiquitination reactions. Using NHL-1 as the E3 in the assays, ubiquitination was observed when both UBC-1 and UBC-13 were present but not with either alone. These data imply that some E2s require dimerization in order to function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
325
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
479-86
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Interactions within the ubiquitin pathway of Caenorhabditis elegans.
pubmed:affiliation
Department of Biological Sciences, University of Alabama in Huntsville, Huntsville, AL 35899, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't