Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport

Markku Aalto, Hans Ronne, Sirkka Keränen

Research output: Contribution to journalArticleScientificpeer-review

327 Citations (Scopus)

Abstract

The yeast SEC1 gene encodes a hydrophilic protein that functions at the terminal stage in secretion. We have cloned two yeast genes, SSO1 and SSO2, which in high copy number can suppress sec1 mutations and also mutations in several other late acting SEC genes, such as SEC3, SEC5, SEC9 and SEC15. SSO1 and SSO2 encode small proteins with N‐terminal hydrophilic domains and C‐terminal hydrophobic tails. The two proteins are 72% identical in sequence and together perform an essential function late in secretion. Sso1p and Sso2p show significant sequence similarity to six other proteins. Two of these, Sed5p and Pep12p, are yeast proteins that function in transport from ER to Golgi and from Golgi to the vacuole, respectively. Also related to Sso1p and Sso2p are three mammalian proteins: epimorphin, syntaxin A/HPC‐1 and syntaxin B. A nematode cDNA product also belongs to the new protein family. The new protein family is thus present in a wide variety of eukaryotic cells, where its members function at different stages in vesicular transport.

Original languageEnglish
Pages (from-to)4095 - 4104
Number of pages10
JournalEMBO Journal
Volume12
Issue number11
DOIs
Publication statusPublished - 1993
MoE publication typeA1 Journal article-refereed

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Qa-SNARE Proteins
Yeast
Membrane Proteins
Yeasts
Proteins
Genes
Syntaxin 1
Mutation
Fungal Proteins
Eukaryotic Cells
Vacuoles
Complementary DNA

Cite this

Aalto, Markku ; Ronne, Hans ; Keränen, Sirkka. / Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport. In: EMBO Journal. 1993 ; Vol. 12, No. 11. pp. 4095 - 4104.
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abstract = "The yeast SEC1 gene encodes a hydrophilic protein that functions at the terminal stage in secretion. We have cloned two yeast genes, SSO1 and SSO2, which in high copy number can suppress sec1 mutations and also mutations in several other late acting SEC genes, such as SEC3, SEC5, SEC9 and SEC15. SSO1 and SSO2 encode small proteins with N‐terminal hydrophilic domains and C‐terminal hydrophobic tails. The two proteins are 72{\%} identical in sequence and together perform an essential function late in secretion. Sso1p and Sso2p show significant sequence similarity to six other proteins. Two of these, Sed5p and Pep12p, are yeast proteins that function in transport from ER to Golgi and from Golgi to the vacuole, respectively. Also related to Sso1p and Sso2p are three mammalian proteins: epimorphin, syntaxin A/HPC‐1 and syntaxin B. A nematode cDNA product also belongs to the new protein family. The new protein family is thus present in a wide variety of eukaryotic cells, where its members function at different stages in vesicular transport.",
author = "Markku Aalto and Hans Ronne and Sirkka Ker{\"a}nen",
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Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport. / Aalto, Markku; Ronne, Hans; Keränen, Sirkka.

In: EMBO Journal, Vol. 12, No. 11, 1993, p. 4095 - 4104.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Yeast syntaxins Sso1p and Sso2p belong to a family of related membrane proteins that function in vesicular transport

AU - Aalto, Markku

AU - Ronne, Hans

AU - Keränen, Sirkka

N1 - Project code: BIO2018

PY - 1993

Y1 - 1993

N2 - The yeast SEC1 gene encodes a hydrophilic protein that functions at the terminal stage in secretion. We have cloned two yeast genes, SSO1 and SSO2, which in high copy number can suppress sec1 mutations and also mutations in several other late acting SEC genes, such as SEC3, SEC5, SEC9 and SEC15. SSO1 and SSO2 encode small proteins with N‐terminal hydrophilic domains and C‐terminal hydrophobic tails. The two proteins are 72% identical in sequence and together perform an essential function late in secretion. Sso1p and Sso2p show significant sequence similarity to six other proteins. Two of these, Sed5p and Pep12p, are yeast proteins that function in transport from ER to Golgi and from Golgi to the vacuole, respectively. Also related to Sso1p and Sso2p are three mammalian proteins: epimorphin, syntaxin A/HPC‐1 and syntaxin B. A nematode cDNA product also belongs to the new protein family. The new protein family is thus present in a wide variety of eukaryotic cells, where its members function at different stages in vesicular transport.

AB - The yeast SEC1 gene encodes a hydrophilic protein that functions at the terminal stage in secretion. We have cloned two yeast genes, SSO1 and SSO2, which in high copy number can suppress sec1 mutations and also mutations in several other late acting SEC genes, such as SEC3, SEC5, SEC9 and SEC15. SSO1 and SSO2 encode small proteins with N‐terminal hydrophilic domains and C‐terminal hydrophobic tails. The two proteins are 72% identical in sequence and together perform an essential function late in secretion. Sso1p and Sso2p show significant sequence similarity to six other proteins. Two of these, Sed5p and Pep12p, are yeast proteins that function in transport from ER to Golgi and from Golgi to the vacuole, respectively. Also related to Sso1p and Sso2p are three mammalian proteins: epimorphin, syntaxin A/HPC‐1 and syntaxin B. A nematode cDNA product also belongs to the new protein family. The new protein family is thus present in a wide variety of eukaryotic cells, where its members function at different stages in vesicular transport.

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