rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
10
|
pubmed:dateCreated |
1998-7-1
|
pubmed:abstractText |
The elaborate and energy-intensive spliceosome assembly pathway belies the seemingly simple chemistry of pre-mRNA splicing. Prp38p was previously identified as a protein required in vivo and in vitro for the first pre-mRNA cleavage reaction catalyzed by the spliceosome. Here we show that Prp38p is a unique component of the U4/U6.U5 tri-small nuclear ribonucleoprotein (snRNP) particle and is necessary for an essential step late in spliceosome maturation. Without Prp38p activity spliceosomes form, but arrest in a catalytically impaired state. Functional spliceosomes shed U4 snRNA before 5' splice-site cleavage. In contrast, Prp38p-defective spliceosomes retain U4 snRNA bound to its U6 snRNA base-pairing partner. Prp38p is the first tri-snRNP-specific protein shown to be dispensable for assembly, but required for conformational changes which lead to catalytic activation of the spliceosome.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0261-4189
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
15
|
pubmed:volume |
17
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2938-46
|
pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
|
pubmed:year |
1998
|
pubmed:articleTitle |
Progression through the spliceosome cycle requires Prp38p function for U4/U6 snRNA dissociation.
|
pubmed:affiliation |
T.H. Morgan School of Biological Sciences, University of Kentucky, Lexington, KY 40506-0225, USA.
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pubmed:publicationType |
Journal Article
|