Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-3-4
pubmed:abstractText
In the yeast Saccharomyces cerevisiae, the splicing of mRNA precursors is disrupted by a severe heat shock. Mild heat treatments prior to severe heat shock protect splicing from disruption, as was previously reported for Drosophila melanogaster. In contrast to D. melanogaster, protein synthesis during the pretreatment is not required to protect splicing in yeast cells. However, protein synthesis is required for the rapid recovery of splicing once it has been disrupted by a sudden severe heat shock. Mutations in two classes of yeast hsp genes affect the pattern of RNA splicing during the heat shock response. First, certain hsp70 mutants, which overproduce other heat shock proteins at normal temperatures, show constitutive protection of splicing at high temperatures and do not require pretreatment. Second, in hsp104 mutants, the recovery of RNA splicing after a severe heat shock is delayed compared with wild-type cells. These results indicate a greater degree of specialization in the protective functions of hsps than has previously been suspected. Some of the proteins (e.g., members of the hsp70 and hsp82 gene families) help to maintain normal cellular processes at higher temperatures. The particular function of hsp104, at least in splicing, is to facilitate recovery of the process once it has been disrupted.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2183028, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2188365, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2421918, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2573430, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2655924, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2674684, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2853609, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2880558, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2943217, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2944601, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2950324, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2962902, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2974799, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-2977088, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3025663, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3201243, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3302675, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3302682, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3336356, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3518952, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3544217, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3588308, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-3952495, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6296115, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6318115, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6325446, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6386178, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6390434, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6421488, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6436685, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6761581, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6826649, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-6994099, http://linkedlifedata.com/resource/pubmed/commentcorrection/1899282-7001447
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0270-7306
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:geneSymbol
hsp104, hsp70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1062-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Heat shock proteins affect RNA processing during the heat shock response of Saccharomyces cerevisiae.
pubmed:affiliation
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't