Abstract
Using differential hybridization, a gene preferentially expressed during entry into stationary phase has been isolated. Subsequent analysis indicated that this gene corresponds to a heat-shock gene. The nucleotide sequence has been determined. It revealed a 332 aminoacid protein. No similarities to any previously known protein have been noted. The protein is very hydrophobic and is predicted to have a membraneous localisation. In agreement with this hypothesis, the analysis of membrane proteins from stationary-phase cells showed that a strain carrying this gene on a multicopy vector overproduces a protein of 30 kDa. This protein was recognized by antibodies directed against the N-terminal portion of the gene product. Considering its induction in response to heat shock and the apparent molecular weight of its product, this gene was designated HSP30.
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Bataillé N, Régnacq M, Boucherie H (1991) Yeast 7:367–378
Belazzi T, Wagner A, Wieser R, Schanz M, Adam G, Hartig A, Ruis H (1991) EMBO J 10:585–592
Bennetzen JL, Hall BD (1982) J Biol Chem 257:3029–3031
Boorstein WR, Craig EA (1990) EMBO J 9:2543–2553
Boucherie H (1985) J Bacteriol 161:386–392
Brand AH, Micklem G, Nasmyth K (1987) Cell 51:709–719
Briggs MS, Gierasch LM (1986) Adv Prot Chem 38:109–181
Buchman AR, Lue NF, Kornberg RD (1988) Mol Cell Biol 8:5086–5099
Cingan AM, Donahue TF (1987) Gene 59:1–18
Finley D, Özkaynak E, Varshavsky A (1987) Cell 48:1035–1046
Iida H, Yahara I (1984) J Cell Biol 99:199–207
Kaufmann E, Geisler N, Weber K (1984) FEBS Lett 170:81–84
Kurtz S, Rossi J, Petko L, Lindquist S (1986) Science 231:1154–1157
Kyte J, Doolitle RF (1982) J Mol Biol 157:105–132
Laemmli UK (1970) Nature 227:680–685
Lis TL, Xiao H, Perisic O (1990) Stress proteins in biology and medicine. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, pp 411–428
McIntosh M, Haynes RH (1986) Mol Cell Biol 6:1711–1721
Maniatis T, Fritsch EF, Sambrook J (1989) Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
Merril CR, Dunau ML, Goldman D (1981) Anal Biochem 110:201–207
Messing J (1983) Methods Enzymol 101:20–78
Mosse MO, Brouillet S, Risler JL, Lazowska J, Slonimski PP (1988) Curr Genet 14 (6):529–535
Nasmith KA, Reed SI (1980) Proc Natl Acad Sci USA 77:2119–2123
Oliver S et al. (1992) Nature 357:38–46
Olmsted JB (1981) J Biol Chem 256:11955–11958
Ozkaynak E, Finley D, Solomon MJ, Varshavsky A (1987) EMBO J 6:1429–1439
Nakayama N, Miyajima A, Arai K (1985) EMBO J 4:2643–2648
Panaretou B, Piper PW (1990) J Gen Microbiol 136:1763–1770
Panaretou B, Piper PW (1992) Eur J Biochem 206:635–640
Proudfoot NJ, Brownlee CG (1976) Nature 263:211–214
Rothblatt JA, Deshaies RJ, Sanders SL, Daum G, Shekman R (1989) J Cell Biol 109:2641–2652
Salder I, Chiang A, Kurihara T, Rothblatt J, Way J, Silver P (1989) J Cell Biol 109:2665–2667
Sanger F, Nicklen S, Coulson AR (1977) Proc Natl Acad Sci USA 74:5463–5467
Smith DB, Johnson KS (1988) Gene 108:31–40
Spalding A, Tuite MF (1989) J Gen Microbiol 135:1037–1045
Tanguay RM (1988) Cell Biol 66:584–593
Tuite MF, Bossier P, Fitch IT (1988) Nucleic Acids Res 16:11845
Ulaszewski S, Grenson M, Goffeau A (1983) Eur J Biochem 130:235–239
Verma R, Iida H, Pardee AB (1988) J Biol Chem 263:8569–8575
Zaret KS, Sherman F (1982) Cell 28:563–573
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Communicated by P. P. Slonimski
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Régnacq, M., Boucherie, H. Isolation and sequence of HSP30, a yeast heat-shock gene coding for a hydrophobic membrane protein. Curr Genet 23, 435–442 (1993). https://doi.org/10.1007/BF00312631
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DOI: https://doi.org/10.1007/BF00312631