She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA

Roy M. Long, Wei Gu, Ellen Lorimer, Robert H. Singer, Pascal Chartrand

Research output: Contribution to journalArticle

151 Citations (Scopus)

Abstract

In Saccharomyces cerevisiae, Ash1p is a specific repressor of transcription that localizes exclusively to daughter cell nuclei through the asymmetric localization of ASH1 mRNA. This localization requires four cis-acting localization elements located in the ASH1 mRNA, five transacting factors, one of which is a myosin, and the actin cytoskeleton. The RNA-binding proteins that interact with these cis-elements remained to be identified. Starting with the 3' most localization element of ASH1 mRNA in the three-hybrid assay, element E3, we isolated a clone corresponding to the C-terminus of She3p. We also found that She3p and She2p interact, and this interaction is essential for the binding of She3p with element E3 in vivo. Moreover, She2p was observed to bind the E3 RNA directly in vitro and each of the ASH1 cis-acting localization elements requires She2p for their localization function. By tethering a She3p-MS2 fusion protein to a reporter RNA containing MS2 binding sites, we observed that She2p is dispensable for She3p-MS2-dependent RNA localization.

Original languageEnglish (US)
Pages (from-to)6592-6601
Number of pages10
JournalEMBO Journal
Volume19
Issue number23
StatePublished - Dec 1 2000

Fingerprint

RNA-Binding Proteins
RNA
Messenger RNA
Transcription
Myosins
Cell Nucleus
Actin Cytoskeleton
Yeast
Saccharomyces cerevisiae
Actins
Assays
Fusion reactions
Clone Cells
Binding Sites
Cells
Proteins

Keywords

  • ASH1
  • MRNA localization
  • RNA-binding proteins
  • Saccharomyces cerevisiae
  • Three-hybrid assay

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Long, R. M., Gu, W., Lorimer, E., Singer, R. H., & Chartrand, P. (2000). She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA. EMBO Journal, 19(23), 6592-6601.

She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA. / Long, Roy M.; Gu, Wei; Lorimer, Ellen; Singer, Robert H.; Chartrand, Pascal.

In: EMBO Journal, Vol. 19, No. 23, 01.12.2000, p. 6592-6601.

Research output: Contribution to journalArticle

Long, RM, Gu, W, Lorimer, E, Singer, RH & Chartrand, P 2000, 'She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA', EMBO Journal, vol. 19, no. 23, pp. 6592-6601.
Long, Roy M. ; Gu, Wei ; Lorimer, Ellen ; Singer, Robert H. ; Chartrand, Pascal. / She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA. In: EMBO Journal. 2000 ; Vol. 19, No. 23. pp. 6592-6601.
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abstract = "In Saccharomyces cerevisiae, Ash1p is a specific repressor of transcription that localizes exclusively to daughter cell nuclei through the asymmetric localization of ASH1 mRNA. This localization requires four cis-acting localization elements located in the ASH1 mRNA, five transacting factors, one of which is a myosin, and the actin cytoskeleton. The RNA-binding proteins that interact with these cis-elements remained to be identified. Starting with the 3' most localization element of ASH1 mRNA in the three-hybrid assay, element E3, we isolated a clone corresponding to the C-terminus of She3p. We also found that She3p and She2p interact, and this interaction is essential for the binding of She3p with element E3 in vivo. Moreover, She2p was observed to bind the E3 RNA directly in vitro and each of the ASH1 cis-acting localization elements requires She2p for their localization function. By tethering a She3p-MS2 fusion protein to a reporter RNA containing MS2 binding sites, we observed that She2p is dispensable for She3p-MS2-dependent RNA localization.",
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AB - In Saccharomyces cerevisiae, Ash1p is a specific repressor of transcription that localizes exclusively to daughter cell nuclei through the asymmetric localization of ASH1 mRNA. This localization requires four cis-acting localization elements located in the ASH1 mRNA, five transacting factors, one of which is a myosin, and the actin cytoskeleton. The RNA-binding proteins that interact with these cis-elements remained to be identified. Starting with the 3' most localization element of ASH1 mRNA in the three-hybrid assay, element E3, we isolated a clone corresponding to the C-terminus of She3p. We also found that She3p and She2p interact, and this interaction is essential for the binding of She3p with element E3 in vivo. Moreover, She2p was observed to bind the E3 RNA directly in vitro and each of the ASH1 cis-acting localization elements requires She2p for their localization function. By tethering a She3p-MS2 fusion protein to a reporter RNA containing MS2 binding sites, we observed that She2p is dispensable for She3p-MS2-dependent RNA localization.

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