The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase.

SIT4 is the catalytic subunit of a type 2A-related protein phosphatase in Saccharomyces cerevisiae that is required for G1 cyclin transcription and for bud formation. SIT4 associates with several high-molecular-mass proteins in a cell cycle-dependent fashion. We purified two SIT4-associated proteins...

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Prif Awduron: Luke, M M, Della Seta, F, Di Como, C J, Sugimoto, H, Kobayashi, R, Arndt, K T
Fformat: Erthygl
Iaith:en
Cyhoeddwyd: 1996
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Research Article
Mynediad Ar-lein:https://ncbi.nlm.nih.gov/pmc/articles/PMC231265/
https://ncbi.nlm.nih.gov/pubmed/8649382
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spelling pubmed-2312652003-10-28 The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase. Luke, M M Della Seta, F Di Como, C J Sugimoto, H Kobayashi, R Arndt, K T Mol Cell Biol Research Article SIT4 is the catalytic subunit of a type 2A-related protein phosphatase in Saccharomyces cerevisiae that is required for G1 cyclin transcription and for bud formation. SIT4 associates with several high-molecular-mass proteins in a cell cycle-dependent fashion. We purified two SIT4-associated proteins, SAP155 and SAP190, and cloned the corresponding genes. By sequence homology, we isolated two additional SAP genes, SAP185 and SAP4. Through such an association is not yet proven for SAP4, each of SAP155, SAP185, and SAP190 physically associates with SIT4 in separate complexes. The SAPs function positively with SIT4, and by several criteria, the loss of all four SAPs is equivalent to the loss of SIT4. The data suggest that the SAPs are not functional in the absence of SIT4 and likewise that SIT4 is not functional in the absence of the SAPs. The SAPs are hyperphoshorylated in cells lacking SIT4, raising the possibility that the SAPs are substrates of SIT4. By sequence similarity, the SAPs fall into two groups, the SAP4/SAP155 group and the SAP185/SAP190 group. Overexpression of a SAP from one group does not suppress the defects due to the loss of the other group. These findings and others indicate that the SAPs have distinct functions. 1996-06 /pmc/articles/PMC231265/ /pubmed/8649382 Text en
institution US National Library of Medicine
collection PubMed Central
language en
format Article
topic Research Article
spellingShingle Research Article
Luke, M M
Della Seta, F
Di Como, C J
Sugimoto, H
Kobayashi, R
Arndt, K T
The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase.
description SIT4 is the catalytic subunit of a type 2A-related protein phosphatase in Saccharomyces cerevisiae that is required for G1 cyclin transcription and for bud formation. SIT4 associates with several high-molecular-mass proteins in a cell cycle-dependent fashion. We purified two SIT4-associated proteins, SAP155 and SAP190, and cloned the corresponding genes. By sequence homology, we isolated two additional SAP genes, SAP185 and SAP4. Through such an association is not yet proven for SAP4, each of SAP155, SAP185, and SAP190 physically associates with SIT4 in separate complexes. The SAPs function positively with SIT4, and by several criteria, the loss of all four SAPs is equivalent to the loss of SIT4. The data suggest that the SAPs are not functional in the absence of SIT4 and likewise that SIT4 is not functional in the absence of the SAPs. The SAPs are hyperphoshorylated in cells lacking SIT4, raising the possibility that the SAPs are substrates of SIT4. By sequence similarity, the SAPs fall into two groups, the SAP4/SAP155 group and the SAP185/SAP190 group. Overexpression of a SAP from one group does not suppress the defects due to the loss of the other group. These findings and others indicate that the SAPs have distinct functions.
author Luke, M M
Della Seta, F
Di Como, C J
Sugimoto, H
Kobayashi, R
Arndt, K T
author_facet Luke, M M
Della Seta, F
Di Como, C J
Sugimoto, H
Kobayashi, R
Arndt, K T
author_sort Luke, M M
title The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase.
title_short The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase.
title_full The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase.
title_fullStr The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase.
title_full_unstemmed The SAP, a new family of proteins, associate and function positively with the SIT4 phosphatase.
title_sort sap, a new family of proteins, associate and function positively with the sit4 phosphatase.
publishDate 1996
url https://ncbi.nlm.nih.gov/pmc/articles/PMC231265/
https://ncbi.nlm.nih.gov/pubmed/8649382
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