RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex

Graydon B. Gonsalvez, Katrina A. Lehmann, Derek K. Ho, Eleni S. Stanitsa, James R. Williamson, Roy M. Long

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

In Saccharomyces cerevisiae, ASH1 mRNA is localized to the tip of daughter cells during anaphase of the cell cycle. ASH1 mRNA localization is dependent on four cis-acting localization elements as well as Myo4p, She2p, and She3p. Myo4p, She2p, and She3p are hypothesized to form a heterotrimeric protein complex that directly transports ASH1 mRNA to daughter cells. She2p is an RNA-binding protein that directly interacts with ASH1 cis-acting localization elements and associates with She3p. Here we report the identification of seven She2p mutants-N36S, R43A, R44A, R52A, R52K, R63A, and R63K-that result in the delocalization of ASH1 mRNA. These mutants are defective for RNA-binding activity but retain the ability to interact with She3p, indicating that a functional She2p RNA-binding domain is not a prerequisite for association with She3p. Furthermore, the nuclear/cytoplasmic distribution for the N36S and R63K She2p mutants is not altered, indicating that nuclear/cytoplasmic trafficking of She2p is independent of RNA-binding activity. Using the N36S and R63K She2p mutants, we observed that in the absence of She2p RNA-binding activity, neither Myo4p nor She3p is asymmetrically sorted to daughter cells. However, in the absence of She2p, Myo4p and She3p can be asymmetrically segregated to daughter cells by artificially tethering mRNA to She3p, implying that the transport and/or anchoring of the Myo4p/She3p complex is dependent on the presence of associated mRNA.

Original languageEnglish (US)
Pages (from-to)1383-1399
Number of pages17
JournalRNA
Volume9
Issue number11
DOIs
StatePublished - Nov 2003

Keywords

  • IST2
  • MRNA localization
  • Myosin
  • RNA-binding protein
  • SHE1/MYO4
  • SHE2
  • SHE3
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Molecular Biology

Fingerprint Dive into the research topics of 'RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex'. Together they form a unique fingerprint.

  • Cite this

    Gonsalvez, G. B., Lehmann, K. A., Ho, D. K., Stanitsa, E. S., Williamson, J. R., & Long, R. M. (2003). RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex. RNA, 9(11), 1383-1399. https://doi.org/10.1261/rna.5120803