RNA localization is a widely utilized strategy employed by cells to spatially restrict protein function. In Saccharomyces cerevisiae asymmetric sorting of mRNA to the bud has been reported for at least 24 mRNAs. The mechanism by which the mRNAs are trafficked to the bud, illustrated by ASH1 mRNA, involves recognition of cis-acting localization elements present in the mRNA by the RNA-binding protein, She2p. The She2p/mRNA complex subsequently associates with the myosin motor protein, Myo4p, through an adapter, She3p. This ribonucleoprotein complex is transported to the distal tip of the bud along polarized actin cables. While the mechanism by which ASH1 mRNA is anchored at the bud tip is unknown, current data point to a role for translation in this process, and the rate of translation of Ash1p during the transport phase is regulated by the cis-acting localization elements. Subcellular sorting of mRNA in yeast is not limited to the bud; certain mRNAs corresponding to nuclear-encoded mitochondrial proteins are specifically sorted to the proximity of mitochondria. Analogous to ASH1 mRNA localization, mitochondrial sorting requires cis-acting elements present in the mRNA, though trans-acting factors involved with this process remain to be identified. This review aims to discuss mechanistic details of mRNA localization in S. cerevisiae.
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RNA
June 2023
Department of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Quebec H3C 3J7, Canada
Messenger RNA (mRNA) localization is an important mechanism controlling local protein synthesis. In budding yeast, asymmetric localization of transcripts such as mRNA to the bud tip depends on the She2 RNA-binding protein. She2 assembles as a tetramer to bind RNA, but the regulation of this process as part of the mRNA locasome is still unclear.
View Article and Find Full Text PDFMicroPubl Biol
February 2023
Centre de Recherche en Biologie cellulaire de Montpellier (CRBM), Université de Montpellier, Centre National de la Recherche Scientifique, 34293 Montpellier CEDEX 05, France.
The auxin-inducible degradation (AID) system can elicit conditional and reversible protein degradation as a tool to assess the role of essential proteins. Indeed, AID enables functional studies without the possibility of adaptation, which can occur with permanent gene deletions. The AID system relies on the addition of auxin molecules, such as indole-3-acetic acid (IAA), as a means to launch the degradation of the protein of interest.
View Article and Find Full Text PDFEcotoxicol Environ Saf
January 2023
College of Life Sciences, Shaanxi Normal University, Xi'an 710119, China. Electronic address:
The transgenerational inheritance of phenotype induced by environmental factors is a new focus in epigenetic research. In this study, Drosophila melanogaster (F) was cultured in the medium containing cadmium (Cd, 4.5 mg/kg) from eggs to adults, and offspring (F-F) were continuously kept in standard medium (without cadmium).
View Article and Find Full Text PDFMicroorganisms
March 2022
Faculty of Biological Science and Technology, Institute of Science and Engineering, Kanazawa University, Kanazawa 920-1192, Japan.
In , the Rpd3L complex contains a histone deacetylase, Rpd3, and the DNA binding proteins, Ume6 and Ash1, and acts as a transcriptional repressor or activator. We previously showed that and are required for the activation of , which encodes a major efflux pump, and pleiotropic drug resistance (PDR) in ρ cells, which lack mitochondrial DNA. However, there are inconsistent reports regarding whether and are required for Pdr5-mediated PDR in ρ cells with mitochondrial DNA.
View Article and Find Full Text PDFBMC Microbiol
November 2021
Faculty of Biological Science and Technology, Institute of Science and Engineering, Kanazawa University, Kanazawa, 920-1164, Japan.
Background: In Saccharomyces cerevisiae, the retrograde signalling pathway is activated in ρ cells, which lack mitochondrial DNA. Within this pathway, the activation of the transcription factor Pdr3 induces transcription of the ATP-binding cassette (ABC) transporter gene, PDR5, and causes pleiotropic drug resistance (PDR). Although a histone deacetylase, Rpd3, is also required for cycloheximide resistance in ρ cells, it is currently unknown whether Rpd3 and its DNA binding partners, Ume6 and Ash1, are involved in the activation of PDR5 transcription and PDR in ρ cells.
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