HSP12, a new small heat shock gene of Saccharomyces cerevisiae: analysis of structure, regulation and function

• Published in: Molecular & general genetics Vol. 223; no. 1; pp. 97 - 106
• Main Authors: Praekelt, U.M, Meacock, P.A
• Format: Journal Article
• Language: English
• Published: Germany 01.08.1990
• Subjects: Amino Acid Sequence; amino acid sequences; Base Sequence; Blotting, Northern; Blotting, Southern; Cloning, Molecular; cyclic AMP; Cyclic AMP - metabolism; DNA; DNA, Fungal - genetics; DNA, Fungal - isolation & purification; Electrophoresis, Polyacrylamide Gel; Exons; gene expression; Gene Expression Regulation, Fungal; genes; Genes, Fungal; genetic regulation; heat shock proteins; heat tolerance; Heat-Shock Proteins - biosynthesis; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; messenger RNA; Molecular Sequence Data; Mutation; Northern blotting; nucleotide sequences; Phosphorylation; polyacrylamide gel electrophoresis; prediction; restriction mapping; Saccharomyces cerevisiae; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - growth & development; Sequence Homology, Nucleic Acid; Southern blotting; Temperature
• ISSN: 0026-8925; 1432-1874
• DOI: 10.1007/bf00315801

We have isolated a new small heat shock gene, HSP12, from Saccharomyces cerevisiae. It encodes a polypeptide of predicted Mr 12 kDa, with structural similarity to other small heat shock proteins. HSP12 gene expression is induced several hundred-fold by heat shock and on entry into stationary phase. HSP12 mRNA is undetectable during exponential growth in rich medium, but low levels are present when cells are grown in minimal medium. Analysis of HSP12 expression in mutants affected in cAMP-dependent protein phosphorylation suggests that the gene is regulated by cAMP as well as heat shock. A disruption of the HSP12 coding region results in the loss of an abundant 14.4 kDa protein present in heat shocked and stationary phase cells. It also leads to the induction of the heat shock response under conditions normally associated with low-level HSP12 expression. The HSP12 disruption has no observable effect on growth at various temperatures, nor on the ability to acquire thermotolerance.