Sargan D R, Tsai M J, O'Malley B W
Biochemistry. 1986 Oct 7;25(20):6252-8. doi: 10.1021/bi00368a062.
cDNA clones encoding a protein that copurifies with the progesterone receptor B subunit but does not bind progesterone have been described [Kulomaa, M. S., Weigel, N. L., Kleinsek, D. A., Beattie, W. G., Conneely, O. M., March, C., Zarucki-Schulz, T., Schrader, W. T., & O'Malley, B. W. (1986) Biochemistry (preceding paper in this issue)]. A full-length sequence for these clones was derived and was found to encode a protein that is structurally unrelated to the progesterone receptor but that contains significant homologies to the previously described heat shock proteins hsp90 of yeast and hsp83a of Drosophila melanogaster. In this paper it is shown that this protein is indeed a heat shock protein. Though the apparent molecular weight of the protein is 108,000 on sodium dodecyl sulfate-polyacrylamide gels, the molecular weight of the polypeptide backbone is 92,000. The steady-state level of gene transcripts as well as the level of protein is inducible by heat shock, but the gene is constitutively expressed in a number of tissues. A previously undescribed heat shock protein of molecular weight 78,000 in these preparations is also reported.
已报道了编码一种与孕酮受体B亚基共纯化但不结合孕酮的蛋白质的cDNA克隆[库洛马,M.S.,韦格尔,N.L.,克莱因塞克,D.A.,比蒂,W.G.,康奈利,O.M.,马奇,C.,扎鲁基 - 舒尔茨,T.,施拉德,W.T.,&奥马利,B.W.(1986年)《生物化学》(本期前一篇论文)]。推导了这些克隆的全长序列,发现其编码的蛋白质在结构上与孕酮受体无关,但与先前描述的酵母热休克蛋白hsp90和黑腹果蝇热休克蛋白hsp83a具有显著同源性。本文表明该蛋白质确实是一种热休克蛋白。虽然该蛋白质在十二烷基硫酸钠 - 聚丙烯酰胺凝胶上的表观分子量为108,000,但多肽主链的分子量为92,000。基因转录本以及蛋白质的稳态水平可被热休克诱导,但该基因在许多组织中组成性表达。还报道了这些制剂中一种先前未描述的分子量为78,000的热休克蛋白。