Yeast SM-like proteins function in mRNA decapping and decay
Article Abstract:
Mutations in seven yeast Sm-like (Lsm) proteins result in inhibition of mRNA decapping, and the seven proteins co-immunoprecipitate with the mRNA decappingenzyme Dcp1.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
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Evidence for an essential non-Watson-Crick interaction between the first and last nucleotides of a nuclear pre-mRNA intron
Article Abstract:
An analysis of the nuclear pre-messenger RNA splicing sites 3' and 5' of the yeast actin intron, Saccharomyces cerevisiae, provides evidence of a non-Watson-Crick interaction between the 3' and 5' splice site guanosines. The 3' site's AG dinucleotide interacts with the 5' site's GU during the second step of splicing and if a mutation has occurred at either site it must be suppressed if the second step of splicing is to continue properly. Therefore, specific nucleotide combinations are required at those two sites.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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An essential component of the decapping enzyme required for normal rates of mRNA turnover
Article Abstract:
Differences in the interaction of the yeast DCP1 decapping enzyme with individual transcripts determines the rate of mmRNA-specific decapping. The activity of Dcp1 on transcripts is affected by proteins that identify specific mRNA features. Also, change in mRNP structure that influences the accessibility of the cap structure to the decapping enzyme, may alter the decapping rate. Dcp1 protein is essential for normal decaying of several unstable and stable yeast mRNAs, and for mRNAs that undergo deadenylation-independent decapping.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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