Asymmetric sorting of ash1p in yeast results from inhibition of translation by localization elements in the mRNA.
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.
Chartrand
Pascal
P
Department of Anatomy and Structural Biology, Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Meng
Xiu Hua
XH
Huttelmaier
Stefan
S
Donato
Damiane
D
Singer
Robert H
RH
D020121:5' Untranslated Regions / Q000235:genetics; D001483:Base Sequence; D004268:DNA-Binding Proteins; D015966:Gene Expression Regulation, Fungal; D017403:In Situ Hybridization; D007700:Kinetics; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis / Q000502:physiology; D012333:RNA, Messenger / Q000737:chemistry / Q000235:genetics*; D012097:Repressor Proteins; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000235:genetics / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016335:Zinc Fingers
D020121:5' Untranslated Regions; C098733:ASH1 protein, S cerevisiae; D004268:DNA-Binding Proteins; D012333:RNA, Messenger; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors