Iwahashi H, Wu Y, Tanguay R M
Laboratoire de Génétique Cellulaire et Moléculaire, Centre de Recherche du CHUL, Ste-Foy, Québec, Canada.
Biochem Biophys Res Commun. 1995 Aug 15;213(2):484-9. doi: 10.1006/bbrc.1995.2157.
Ssb1p and ssb2p are two members of the hsp70 family in yeast. Up to now there has been no evidence to indicate any differences between these two members of the hsp70 family, and it was suggested that ssb1p and ssb2p were 99% identical. Here we show that an antibody prepared against the C-terminal domain of human hsp71 recognizes specifically ssb1p out of the eight hsp(c)70s in Saccharomyces cerevisiae. An amino acid peptide sequence at the C-terminal end (VTATDKSTGK) is suggested to be the sequence which has high homology between ssb1p and hu-hsp71 and to be responsible for the specificity of recognition of this unique member of the hsp70 family. Using this antibody in immunoblot assays, we have determined the cellular content of ssb1p after heat shock and at different growth temperatures. Ssb1p is shown to be degraded during heat shock treatment while it shows a higher level of expression at low temperatures.
Ssb1p和Ssb2p是酵母中hsp70家族的两个成员。到目前为止，没有证据表明hsp70家族的这两个成员之间存在任何差异，有人认为Ssb1p和Ssb2p的同源性为99%。在此我们表明，一种针对人hsp71 C末端结构域制备的抗体，能从酿酒酵母的八个hsp(c)70中特异性识别Ssb1p。有人认为C末端的氨基酸肽序列（VTATDKSTGK）是Ssb1p和人hsp71之间具有高度同源性的序列，并且是负责识别hsp70家族这一独特成员的特异性序列。在免疫印迹分析中使用这种抗体，我们测定了热休克后以及在不同生长温度下Ssb1p的细胞含量。结果显示，Ssb1p在热休克处理过程中会被降解，而在低温下其表达水平较高。
