Abstract
ASH1 mRNA localizes at the bud tip of late-anaphase yeast, resulting in accumulation of Ash1p in the daughter nucleus. We show that disruption of the secondary structure, but not the protein coding, of all four ASH1 localization elements resulted in RNA and protein delocalization. Localization of both was incrementally restored by replacement of each of the four elements. However, transposition of the elements to the 3'UTR reinstated the RNA, but not the protein, localization. Interestingly, the mutant ASH1 mRNA was translated more efficiently, suggesting that asymmetry of Ash1p resulted from translational inhibition by the localization elements. In support of this, Ash1p asymmetry could be rescued by slowing its translation.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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5' Untranslated Regions / genetics
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Base Sequence
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DNA-Binding Proteins*
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Gene Expression Regulation, Fungal
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In Situ Hybridization
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Kinetics
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Molecular Sequence Data
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Nucleic Acid Conformation
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Protein Biosynthesis* / physiology
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RNA, Messenger / chemistry
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RNA, Messenger / genetics*
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Repressor Proteins*
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / physiology*
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Saccharomyces cerevisiae Proteins*
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Zinc Fingers
Substances
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5' Untranslated Regions
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ASH1 protein, S cerevisiae
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DNA-Binding Proteins
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RNA, Messenger
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Repressor Proteins
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Saccharomyces cerevisiae Proteins
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Transcription Factors