Regulation of cation transport in Saccharomyces cerevisiae by the salt tolerance gene HAL3.
Dynamic regulation of ion transport is essential for homeostasis as cells confront changes in their environment. The gene HAL3 encodes a novel component of this regulatory circuit in the yeast Saccharomyces cerevisiae. Overexpression of HAL3 improves growth of wild-type cells exposed to toxic concentrations of sodium and lithium and suppresses the salt sensitivity conferred by mutation of the calcium-dependent protein phosphatase calcineurin. Null mutants of HAL3 display salt sensitivity. The sequence of HAL3 gives little clue to its function. However, alterations in intracellular cation concentrations associated with changes in HAL3 expression suggest that HAL3 activity may directly increase cytoplasmic K+ and decrease Na+ and Li+. Cation efflux in S. cerevisiae is mediated by the P-type ATPase encoded by the ENA1/PMR24 gene, a putative plasma membrane Na+ pump whose expression is salt induced. Acting in concert with calcineurin, HAL3 is necessary for full activation of ENA1 expression. This functional complementarity is also reflected in the participation of both proteins in recovery from alpha-factor-induced growth arrest. Recently, HAL3 was isolated as a gene (named SIS2) which when overexpressed partially relieves loss of transcription of G1 cyclins in mutants lacking the protein phosphatase Sit4p. Therefore, HAL3 influences cell cycle control and ion homeostasis, acting in parallel to the protein phosphatases Sit4p and calcineurin.
Ferrando
A
A
Instituto de Biologia Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, Spain.
Kron
S J
SJ
Rios
G
G
Fink
G R
GR
Serrano
R
R
D000251:Adenosine Triphosphatases / Q000502:physiology; D000595:Amino Acid Sequence; D001483:Base Sequence; D019703:Calcineurin; D002148:Calmodulin-Binding Proteins / Q000235:genetics / Q000502:physiology; D027682:Cation Transport Proteins; D002414:Cations, Monovalent / Q000378:metabolism*; D018797:Cell Cycle Proteins; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000378:metabolism; D004352:Drug Resistance, Microbial; D005656:Fungal Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D005800:Genes, Fungal / Q000235:genetics* / Q000502:physiology; D006706:Homeostasis; D017136:Ion Transport / Q000187:drug effects; D007700:Kinetics; D008094:Lithium / Q000378:metabolism; D008969:Molecular Sequence Data; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000502:physiology; D011188:Potassium / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D017422:Sequence Analysis, DNA; D012964:Sodium / Q000378:metabolism; D012965:Sodium Chloride / Q000494:pharmacology*; D000254:Sodium-Potassium-Exchanging ATPase
D002148:Calmodulin-Binding Proteins; D027682:Cation Transport Proteins; D002414:Cations, Monovalent; D018797:Cell Cycle Proteins; C086375:ENA1 protein, S cerevisiae; D005656:Fungal Proteins; C092936:SIS2 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D012965:Sodium Chloride; D008094:Lithium; D012964:Sodium; D019703:Calcineurin; D010749:Phosphoprotein Phosphatases; D000251:Adenosine Triphosphatases; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium