Linked Life Data

8808631

Source:http://linkedlifedata.com/resource/pubmed/id/8808631

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1996-12-10
pubmed:abstractText
The eukaryotic 20S proteasome is responsible for the degradation of many cellular proteins, but how it is assembled and how its distinct active sites are formed are not understood. Like other proteasome subunits, the yeast Doa3 protein is synthesized in precursor form. We show that the N-terminal propeptide is required for Doa3 incorporation into the proteasome and, remarkably, that the propeptide functions in trans, suggesting it serves a chaperone-like function in proteasome biogenesis. Propeptide processing is not required for proteasome assembly but is needed for maturation of a specific subset of active sites. The likely nucleophile for these sites is provided by the N-terminal threonine of mature Doa3. Additional data indicate that precursor processing is autocatalytic and requires association of the two halves of the proteasome particle, thereby preventing formation of proteolytic sites until the central hydrolytic chamber has been sealed off from the rest of the cell.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
961-72
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, The University of Chicago, Illinois 60637, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.