Heat Treatment of Small Heat Shock Proteins α-Crystallin and Hsp16.3: Structural Changes vs. Chaperone-like Activity

Small heat shock proteins are a conserved,abundant and ubiquitious protein family[1] . Theyhave been detected in all types of organisms,including archaea,bacteria,and eukarya.In spiteof a relatively low overall homology betweendifferent members,they are grouped togetherbased on (a) containing a conservedα- crystallindomain that is preceded by a variable N- terminalregion and followed by an unconserved C- terminalsequence;(b) consisting of mainlyβ- sheets in thesecondary structure;and (c) for…     

Hsp16.3中一个高度保守疏水残基的定点突变

结核杆菌小分子热休克蛋白Ｈｓｐ１６．３为一由三个三聚体组成的寡聚蛋白,并具有分子伴娘活性（Ｃｈａｎｇｅｔａｌ．,Ｊ．Ｂｉｏｌ．Ｃｈｅｍ．,１９９６,２７１：７２１８～７２２３）。为研究高度保守疏水片段中高度保守疏水亮氨酸残基（Ｌｅｕ１２１）对寡聚体结构和活性的影响,该残基被分别定点突变成天冬氨酸（Ａｓｐ）、天冬酰胺（Ａｓｎ）、缬氨酸（Ｖａｌ）和丙氨酸（Ａｌａ）等。结果发现当Ｌｅｕ１２１被突变成Ｖａｌ和Ａｌａ时,通过ＳＤＳ－ＰＡＧＥ凝胶电泳检测仍可见重组蛋白在大肠杆菌中的高水平表达,而当被突变成Ａｓｐ和Ａｓｎ时,在ＳＤＳ－ＰＡＧＥ胶上,见不到Ｈｓｐ１６．３蛋白带。表明该残基可能对寡聚蛋白的结构稳定起重要作用。