Linked Life Data

8702624

Source:http://linkedlifedata.com/resource/pubmed/id/8702624

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
1996-9-16
pubmed:abstractText
Rat Nopp140, a nonribosomal protein of the nucleolus and coiled bodies, was characterized as one of the most highly phosphorylated proteins in the cell. Based on its subcellular location, its nuclear localization signal binding capacity, and its shuttling between the nucleolus and the cytoplasm, Nopp140 was proposed to function as a chaperone in ribosome biogenesis. This study shows that casein kinase II phosphorylates Nopp140 to its unusual high degree and identifies the yeast SRP40 gene product as immunologically and structurally related to rat Nopp140. SRP40 encodes an acidic (pI = 3. 9), serine-rich (49%) protein of 41 kDa whose carboxyl terminus exhibits 59% sequence identity to that of Nopp140. SRP40 localizes to the yeast nucleolus and is required at a specific cellular concentration for optimal growth as indicated by the negative effect on cell growth of both overexpression and deletion of its gene. Like Nopp140, SRP40 is phosphorylated by casein kinase II, but to a much lesser extent. While the parallels between these two proteins suggest that SRP40 is the bona fide yeast Nopp140 homolog, their disparities reflect the differences in nucleolar dynamics and regulation of ribosome biogenesis between yeast and vertebrates.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19376-84
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Comparison of the rat nucleolar protein nopp140 with its yeast homolog SRP40. Differential phosphorylation in vertebrates and yeast.
pubmed:affiliation
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.