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PMID: 10368187 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Sac3, an Snf1-like serine/threonine kinase that positively and negatively regulates the responses of Chlamydomonas to sulfur limitation.

The Plant cell ·Vol. 11 ·No. 6 ·1999-06-00 ·Pages 1179-90

Davies JP, Yildiz FH, Grossman AR

Abstract

The Sac3 gene product of Chlamydomonas positively and negatively regulates the responses of the cell to sulfur limitation. In wild-type cells, arylsulfatase activity is detected only during sulfur limitation. The sac3 mutant expresses arylsulfatase activity even when grown in nutrient-replete medium, which suggests that the Sac3 protein has a negative effect on the induction of arylsulfatase activity. In contrast to its effect on arylsulfatase activity, Sac3 positively regulates the high-affinity sulfate transport system-the sac3 mutant is unable to fully induce high-affinity sulfate transport during sulfur limitation. We have complemented the sac3 mutant and cloned a cDNA copy of the Sac3 gene. The deduced amino acid sequence of the Sac3 gene product is similar to the catalytic domain of the yeast Snf1 family of serine/threonine kinases and is therefore classified as a Snf1-related kinase (SnRK). Specifically, Sac3 falls within the SnRK2 subfamily of kinases from vascular plants. In addition to the 11 subdomains common to Snf1-like serine/threonine kinases, Sac3 and the plant kinases have two additional subdomains and a highly acidic C-terminal region. The role of Sac3 in the signal transduction system that regulates the responses of Chlamydomonas to sulfur limitation is discussed.

MeSH Terms
Amino Acid Sequence Animals Arylsulfatases/metabolism Catalytic Domain Chlamydomonas reinhardtii/enzymology,genetics,physiology Culture Media Homeostasis Molecular Sequence Data Mutagenesis Phylogeny Plant Proteins/chemistry,genetics Polymorphism, Genetic Protein Serine-Threonine Kinases/chemistry,genetics,metabolism Sequence Alignment Sequence Homology, Amino Acid Sulfur/metabolism
Chemicals
Culture Media Plant Proteins Sulfur Sac3 protein kinase Protein Serine-Threonine Kinases Arylsulfatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Davies J P
Department of Botany, 353 Bessey Hall, Iowa State University, Ames, Iowa 50011-1020, USA. jdavies@iastate.edu
Yildiz F H
Grossman A R
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Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1040-4651
DOI
10.1105/tpc.11.6.1179
Email
jdavies@iastate.edu
Published
1999-06-00
Pages
1179-90
Language
English
Region
England
NLM ID
9208688
PMCID
PMC144238
Subset
IM
External Links
PubMed source DOI: 10.1105/tpc.11.6.1179 PMC Full Text View journal details
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