Linked Life Data

19245792

Source:http://linkedlifedata.com/resource/pubmed/id/19245792

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-3-20
pubmed:abstractText
NEDD8 is a small ubiquitin-like protein that modifies target proteins in a reaction similar to ubiquitination. In this reaction, three enzymes are required and sufficient: NEDD8 activating E1-like enzyme (APP-BP1/Uba3), NEDD8-specific E2 enzyme (Ubc12) and RING-finger protein ROC1 (NEDD8 E3 ligase). Unlike ubiquitin, which is well known to form poly-ubiquitin chain, little is known about the formation of poly-NEDD8 chain. Here we show the mechanism of poly-NEDD8 chain formation on Cullin-1 using a complete in vitro reconstituted NEDD8 conjugation system. Intriguingly, poly-NEDD8 chain was build up on catalytic Cysteine residue of Ubc12. Furthermore, Ubc12 formed poly-NEDD8 chain without the activity of ROC1. Rather ROC1 mutant, defective for ubiquitin ligase activity, dramatically enhanced the poly-NEDD8 chain formation. In turn, ROC1 was essential for the transfer of poly-NEDD8 chain from Ubc12 to Cul-1. These results suggest the important regulatory role of ROC1 for poly-NEDD8 chain formation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
10
pubmed:volume
381
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
443-7
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The mechanism of poly-NEDD8 chain formation in vitro.
pubmed:affiliation
Department of Molecular Biology, Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8577, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't