The Saccharomyces cerevisiae gene SDS22 encodes a potential regulator of the mitotic function of yeast type 1 protein phosphatase

Author:

MacKelvie S H1,Andrews P D1,Stark M J1

Affiliation:

1. Department of Biochemistry, University of Dundee, United Kingdom.

Abstract

In higher eukaryotes, the activity and specificity of the type 1 protein serine-threonine phosphatase (PP1) catalytic subunit is thought to be controlled by its association with a number of regulatory or targeting subunits. Here we describe the characterization of a gene encoding one such potential polypeptide in the yeast Saccharomyces cerevisiae. The gene which we have isolated (termed SDS22) encodes a product with a high degree of sequence identity to the fission yeast sds22 protein, a known regulator of the mitotic function of PP1 in Schizosaccharomyces pombe. Using two different criteria, we have demonstrated that Sds22p and the catalytic subunit of PP1 (Glc7p) interact in yeast cells. We have also generated a temperature-sensitive allele of GLC7 (glc7-12) which causes a block to the completion of mitosis at the restrictive temperature. Additional copies of SDS22 lead to allele-specific suppression of the glc7-12 mutant, strongly suggesting that the interaction between the two proteins is of functional significance. Sds22p is therefore likely to be the second example of a PP1 regulatory subunit identified in S. cerevisiae.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

Reference71 articles.

1. Alessi D. L. K. MacDougall M. M. Sola M. Ikebe and P. Cohen. 1992. The control of protein phosphatase 1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase

2. Eur. J. Biochem. 210:1023-1035.

3. Andrews P. D. P. M. McDonald and M. J. R. Stark. Glc8p interacts with the Saccharomyces cerevisiae protein phosphatase 1 catalytic subunit and is a yeast inhibitor 2 homologue. Submitted for publication.

4. Andrews P. D. and M. J. R. Stark. Unpublished data.

5. .Arndt K. T. Unpublished data.

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3