The Highly Conserved Protein Methyltransferase, Skb1, Is a Mediator of Hyperosmotic Stress Response in the Fission Yeast Schizosaccharomyces pombe

Shilai Bao, Yibing Qyang, Peirong Yang, HyeWon Kim, Hongyan Du, Geoffrey Bartholomeusz, Jenny Henkel, Ruth Pimental, Fulvia Verde, Stevan Marcus

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

The p21-activated kinase, Shk1, is required for cell viability, establishment and maintenance of cell polarity, and proper mating response in the fission yeast, Schizosaccharomyces pombe. Previous genetic studies suggested that a presumptive protein methyltransferase, Skb1, functions as a positive modulator of Shk1. However, unlike Shk1, Skb1 is not required for viability or mating of S. pombe cells and contributes only modestly to the regulation of cell morphology under normal growth conditions. Here we demonstrate that Skb1 plays a more significant role in regulating cell growth and polarity under conditions of hyperosmotic stress. We provide evidence that the inability of skb1Δ cells to properly maintain cell polarity in hyperosmotic conditions results from inefficient subcellular targeting of F-actin. We show that Skb1 localizes to cell ends, sites of septation, and nuclei of S. pombe cells. Hyperosmotic shock results in substantial delocalization of Skb1 from cell ends and nuclei, as well as stimulation of Skb1 protein methyltransferase activity. Taken together, our results demonstrate a new role for Skb1 as a mediator of hyperosmotic stress response in fission yeast. We show that the protein methyltransferase activity of the human Skb1 homolog, Skb1Hs, is also stimulated by hyperosmotic stress in fission yeast, providing evidence for evolutionary conservation of a role for Skb1-related proteins as mediators of hyperosmotic stress response, as well as mechanisms involved in regulating this novel class of protein methyltransferases.

Original languageEnglish
Pages (from-to)14549-14552
Number of pages4
JournalJournal of Biological Chemistry
Volume276
Issue number18
DOIs
StatePublished - May 4 2001

Fingerprint

Protein Methyltransferases
Schizosaccharomyces
Yeast
Cell Polarity
Cells
p21-Activated Kinases
Cell growth
Modulators
Actins
Conservation
Growth
Cell Nucleus
Human Activities
Shock
Cell Survival
Maintenance
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

The Highly Conserved Protein Methyltransferase, Skb1, Is a Mediator of Hyperosmotic Stress Response in the Fission Yeast Schizosaccharomyces pombe. / Bao, Shilai; Qyang, Yibing; Yang, Peirong; Kim, HyeWon; Du, Hongyan; Bartholomeusz, Geoffrey; Henkel, Jenny; Pimental, Ruth; Verde, Fulvia; Marcus, Stevan.

In: Journal of Biological Chemistry, Vol. 276, No. 18, 04.05.2001, p. 14549-14552.

Research output: Contribution to journalArticle

Bao, Shilai ; Qyang, Yibing ; Yang, Peirong ; Kim, HyeWon ; Du, Hongyan ; Bartholomeusz, Geoffrey ; Henkel, Jenny ; Pimental, Ruth ; Verde, Fulvia ; Marcus, Stevan. / The Highly Conserved Protein Methyltransferase, Skb1, Is a Mediator of Hyperosmotic Stress Response in the Fission Yeast Schizosaccharomyces pombe. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 18. pp. 14549-14552.
@article{5ab0cc09c80b4975814595254758a41b,
title = "The Highly Conserved Protein Methyltransferase, Skb1, Is a Mediator of Hyperosmotic Stress Response in the Fission Yeast Schizosaccharomyces pombe",
abstract = "The p21-activated kinase, Shk1, is required for cell viability, establishment and maintenance of cell polarity, and proper mating response in the fission yeast, Schizosaccharomyces pombe. Previous genetic studies suggested that a presumptive protein methyltransferase, Skb1, functions as a positive modulator of Shk1. However, unlike Shk1, Skb1 is not required for viability or mating of S. pombe cells and contributes only modestly to the regulation of cell morphology under normal growth conditions. Here we demonstrate that Skb1 plays a more significant role in regulating cell growth and polarity under conditions of hyperosmotic stress. We provide evidence that the inability of skb1Δ cells to properly maintain cell polarity in hyperosmotic conditions results from inefficient subcellular targeting of F-actin. We show that Skb1 localizes to cell ends, sites of septation, and nuclei of S. pombe cells. Hyperosmotic shock results in substantial delocalization of Skb1 from cell ends and nuclei, as well as stimulation of Skb1 protein methyltransferase activity. Taken together, our results demonstrate a new role for Skb1 as a mediator of hyperosmotic stress response in fission yeast. We show that the protein methyltransferase activity of the human Skb1 homolog, Skb1Hs, is also stimulated by hyperosmotic stress in fission yeast, providing evidence for evolutionary conservation of a role for Skb1-related proteins as mediators of hyperosmotic stress response, as well as mechanisms involved in regulating this novel class of protein methyltransferases.",
author = "Shilai Bao and Yibing Qyang and Peirong Yang and HyeWon Kim and Hongyan Du and Geoffrey Bartholomeusz and Jenny Henkel and Ruth Pimental and Fulvia Verde and Stevan Marcus",
year = "2001",
month = "5",
day = "4",
doi = "10.1074/jbc.C100096200",
language = "English",
volume = "276",
pages = "14549--14552",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "18",

}

TY - JOUR

T1 - The Highly Conserved Protein Methyltransferase, Skb1, Is a Mediator of Hyperosmotic Stress Response in the Fission Yeast Schizosaccharomyces pombe

AU - Bao, Shilai

AU - Qyang, Yibing

AU - Yang, Peirong

AU - Kim, HyeWon

AU - Du, Hongyan

AU - Bartholomeusz, Geoffrey

AU - Henkel, Jenny

AU - Pimental, Ruth

AU - Verde, Fulvia

AU - Marcus, Stevan

PY - 2001/5/4

Y1 - 2001/5/4

N2 - The p21-activated kinase, Shk1, is required for cell viability, establishment and maintenance of cell polarity, and proper mating response in the fission yeast, Schizosaccharomyces pombe. Previous genetic studies suggested that a presumptive protein methyltransferase, Skb1, functions as a positive modulator of Shk1. However, unlike Shk1, Skb1 is not required for viability or mating of S. pombe cells and contributes only modestly to the regulation of cell morphology under normal growth conditions. Here we demonstrate that Skb1 plays a more significant role in regulating cell growth and polarity under conditions of hyperosmotic stress. We provide evidence that the inability of skb1Δ cells to properly maintain cell polarity in hyperosmotic conditions results from inefficient subcellular targeting of F-actin. We show that Skb1 localizes to cell ends, sites of septation, and nuclei of S. pombe cells. Hyperosmotic shock results in substantial delocalization of Skb1 from cell ends and nuclei, as well as stimulation of Skb1 protein methyltransferase activity. Taken together, our results demonstrate a new role for Skb1 as a mediator of hyperosmotic stress response in fission yeast. We show that the protein methyltransferase activity of the human Skb1 homolog, Skb1Hs, is also stimulated by hyperosmotic stress in fission yeast, providing evidence for evolutionary conservation of a role for Skb1-related proteins as mediators of hyperosmotic stress response, as well as mechanisms involved in regulating this novel class of protein methyltransferases.

AB - The p21-activated kinase, Shk1, is required for cell viability, establishment and maintenance of cell polarity, and proper mating response in the fission yeast, Schizosaccharomyces pombe. Previous genetic studies suggested that a presumptive protein methyltransferase, Skb1, functions as a positive modulator of Shk1. However, unlike Shk1, Skb1 is not required for viability or mating of S. pombe cells and contributes only modestly to the regulation of cell morphology under normal growth conditions. Here we demonstrate that Skb1 plays a more significant role in regulating cell growth and polarity under conditions of hyperosmotic stress. We provide evidence that the inability of skb1Δ cells to properly maintain cell polarity in hyperosmotic conditions results from inefficient subcellular targeting of F-actin. We show that Skb1 localizes to cell ends, sites of septation, and nuclei of S. pombe cells. Hyperosmotic shock results in substantial delocalization of Skb1 from cell ends and nuclei, as well as stimulation of Skb1 protein methyltransferase activity. Taken together, our results demonstrate a new role for Skb1 as a mediator of hyperosmotic stress response in fission yeast. We show that the protein methyltransferase activity of the human Skb1 homolog, Skb1Hs, is also stimulated by hyperosmotic stress in fission yeast, providing evidence for evolutionary conservation of a role for Skb1-related proteins as mediators of hyperosmotic stress response, as well as mechanisms involved in regulating this novel class of protein methyltransferases.

UR - http://www.scopus.com/inward/record.url?scp=0035805617&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035805617&partnerID=8YFLogxK

U2 - 10.1074/jbc.C100096200

DO - 10.1074/jbc.C100096200

M3 - Article

VL - 276

SP - 14549

EP - 14552

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 18

ER -