Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation

Jussi Jäntti, Markku Aalto, Mattias Öyen, Lena Sundqvist, Sirkka Keränen, Hans Ronne (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

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Abstract

The duplicated genes SSO1 and SSO2 encode yeast homologues of syntaxin 1 and perform an essential function during fusion of secretory vesicles at the plasma membrane. We have used in vitro mutagenesis to obtain a temperature-sensitive SSO2 allele, sso2-1, in which a conserved arginine has been changed to a lysine. A yeast strain that lacks SSO1 and carries the sso2-1 allele ceases growth and accumulates secretory vesicles at the restrictive temperature. Interestingly, the strain also has a pronounced phenotype at the permissive temperature, causing a defect in bud neck closure that prevents separation of mother and daughter cells. The same mutation was introduced into SSO1, producing the sso1-1 allele, which also has a temperature-sensitive phenotype, although less pronounced than sso2-1. A screen for high copy number suppressors of sso2-1 yielded three genes that are involved in the terminal step of secretion: SNC1, SNC2 and SEC9. The sso1-1 mutation interacts synthetically with a disruption of the MSO1 gene, which encodes a Sec1p interacting protein. Interestingly, we further found that both MSO1 and SSO1, but not SSO2, are required for sporulation. This difference is not due to differential expression, since SSO2 expressed from the SSO1 promoter failed to restore sporulation. We conclude that a functional difference exists between the Sso1 and Sso2 proteins, with the former being specifically required during sporulation.
Original languageEnglish
Pages (from-to)409-420
JournalJournal of Cell Science
Volume115
Issue number2
Publication statusPublished - 2002
MoE publication typeA1 Journal article-refereed

Fingerprint

Syntaxin 1
Yeasts
Mutation
Temperature
Alleles
Secretory Vesicles
Genes
Phenotype
Mutagenesis
Lysine
Arginine
Proteins
Stem Cells
Cell Membrane
Growth

Keywords

  • Vesicular transport
  • MSO1
  • SSO1
  • SSO2
  • Secretion
  • SNARE
  • Sporulation
  • Syntaxin

Cite this

@article{952ddf8de6a8403a84e3e338231016d0,
title = "Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation",
abstract = "The duplicated genes SSO1 and SSO2 encode yeast homologues of syntaxin 1 and perform an essential function during fusion of secretory vesicles at the plasma membrane. We have used in vitro mutagenesis to obtain a temperature-sensitive SSO2 allele, sso2-1, in which a conserved arginine has been changed to a lysine. A yeast strain that lacks SSO1 and carries the sso2-1 allele ceases growth and accumulates secretory vesicles at the restrictive temperature. Interestingly, the strain also has a pronounced phenotype at the permissive temperature, causing a defect in bud neck closure that prevents separation of mother and daughter cells. The same mutation was introduced into SSO1, producing the sso1-1 allele, which also has a temperature-sensitive phenotype, although less pronounced than sso2-1. A screen for high copy number suppressors of sso2-1 yielded three genes that are involved in the terminal step of secretion: SNC1, SNC2 and SEC9. The sso1-1 mutation interacts synthetically with a disruption of the MSO1 gene, which encodes a Sec1p interacting protein. Interestingly, we further found that both MSO1 and SSO1, but not SSO2, are required for sporulation. This difference is not due to differential expression, since SSO2 expressed from the SSO1 promoter failed to restore sporulation. We conclude that a functional difference exists between the Sso1 and Sso2 proteins, with the former being specifically required during sporulation.",
keywords = "Vesicular transport, MSO1, SSO1, SSO2, Secretion, SNARE, Sporulation, Syntaxin",
author = "Jussi J{\"a}ntti and Markku Aalto and Mattias {\"O}yen and Lena Sundqvist and Sirkka Ker{\"a}nen and Hans Ronne",
year = "2002",
language = "English",
volume = "115",
pages = "409--420",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "Company of Biologists Ltd",
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}

Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation. / Jäntti, Jussi; Aalto, Markku; Öyen, Mattias; Sundqvist, Lena; Keränen, Sirkka; Ronne, Hans (Corresponding Author).

In: Journal of Cell Science, Vol. 115, No. 2, 2002, p. 409-420.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation

AU - Jäntti, Jussi

AU - Aalto, Markku

AU - Öyen, Mattias

AU - Sundqvist, Lena

AU - Keränen, Sirkka

AU - Ronne, Hans

PY - 2002

Y1 - 2002

N2 - The duplicated genes SSO1 and SSO2 encode yeast homologues of syntaxin 1 and perform an essential function during fusion of secretory vesicles at the plasma membrane. We have used in vitro mutagenesis to obtain a temperature-sensitive SSO2 allele, sso2-1, in which a conserved arginine has been changed to a lysine. A yeast strain that lacks SSO1 and carries the sso2-1 allele ceases growth and accumulates secretory vesicles at the restrictive temperature. Interestingly, the strain also has a pronounced phenotype at the permissive temperature, causing a defect in bud neck closure that prevents separation of mother and daughter cells. The same mutation was introduced into SSO1, producing the sso1-1 allele, which also has a temperature-sensitive phenotype, although less pronounced than sso2-1. A screen for high copy number suppressors of sso2-1 yielded three genes that are involved in the terminal step of secretion: SNC1, SNC2 and SEC9. The sso1-1 mutation interacts synthetically with a disruption of the MSO1 gene, which encodes a Sec1p interacting protein. Interestingly, we further found that both MSO1 and SSO1, but not SSO2, are required for sporulation. This difference is not due to differential expression, since SSO2 expressed from the SSO1 promoter failed to restore sporulation. We conclude that a functional difference exists between the Sso1 and Sso2 proteins, with the former being specifically required during sporulation.

AB - The duplicated genes SSO1 and SSO2 encode yeast homologues of syntaxin 1 and perform an essential function during fusion of secretory vesicles at the plasma membrane. We have used in vitro mutagenesis to obtain a temperature-sensitive SSO2 allele, sso2-1, in which a conserved arginine has been changed to a lysine. A yeast strain that lacks SSO1 and carries the sso2-1 allele ceases growth and accumulates secretory vesicles at the restrictive temperature. Interestingly, the strain also has a pronounced phenotype at the permissive temperature, causing a defect in bud neck closure that prevents separation of mother and daughter cells. The same mutation was introduced into SSO1, producing the sso1-1 allele, which also has a temperature-sensitive phenotype, although less pronounced than sso2-1. A screen for high copy number suppressors of sso2-1 yielded three genes that are involved in the terminal step of secretion: SNC1, SNC2 and SEC9. The sso1-1 mutation interacts synthetically with a disruption of the MSO1 gene, which encodes a Sec1p interacting protein. Interestingly, we further found that both MSO1 and SSO1, but not SSO2, are required for sporulation. This difference is not due to differential expression, since SSO2 expressed from the SSO1 promoter failed to restore sporulation. We conclude that a functional difference exists between the Sso1 and Sso2 proteins, with the former being specifically required during sporulation.

KW - Vesicular transport

KW - MSO1

KW - SSO1

KW - SSO2

KW - Secretion

KW - SNARE

KW - Sporulation

KW - Syntaxin

M3 - Article

VL - 115

SP - 409

EP - 420

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 2

ER -