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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1987-3-11
|
| pubmed:abstractText |
In the filamentous fungus Achlya ambisexualis, heat shock resulted in a rapid reduction in the rate of protein synthesis. This was accompanied by dephosphorylation of a prominent basic 30 kD protein associated with the small subunit of Achlya ribosomes and which may be analogous to ribosomal protein S6 of vertebrates. A large ribosomal subunit protein with a relative molecular weight (MW) of 24,500 exhibited increased phosphorylation during heat shock, while a second large subunit protein having a relative MW of 22,000 was dephosphorylated. Several proteins which could be dissociated from Achlya ribosomes by 0.5 M KCl also exhibited altered patterns of phosphorylation during heat shock. These KCl-soluble proteins included proteins at 50, 21, 20 and 19 kD, which exhibited decreased phosphorylation with heat shock and proteins at 32 and 23.5 kD, which exhibited increased phosphorylation with heat shock. Such alterations in the phosphorylation of components of the Achlya translational apparatus may be involved in the qualitative and quantitative changes in protein synthesis which are observed with heat shock in Achlya.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0014-4827
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
168
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
325-37
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading | |
| pubmed:year |
1987
|
| pubmed:articleTitle |
Heat-shock-induced changes in the phosphorylation of ribosomal and ribosome-associated proteins in the filamentous fungus Achlya ambisexualis.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|