MUTATIONS IN LAMBDA-REPRESSORS AMINO-TERMINAL DOMAIN - IMPLICATIONS FOR PROTEIN STABILITY AND DNA-BINDING
MUTATIONS IN LAMBDA-REPRESSORS AMINO-TERMINAL DOMAIN - IMPLICATIONS FOR PROTEIN STABILITY AND DNA-BINDING
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DOI：
10.1073/pnas.80.9.2676
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发表时间：
1983-01-01
期刊：
影响因子：
--
通讯作者：
SAUER, RT
中科院分区：
文献类型：
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作者：
HECHT, MH;NELSON, HCM;SAUER, RT
对λ阻遏蛋白氨基末端结构域中52种不同的单氨基酸替换的DNA结合特性进行了表征。纯化了7种带有改变溶剂暴露侧链的突变的蛋白质。这些突变阻遏蛋白的氨基末端结构域发生折叠，并且在热稳定性方面与野生型氨基末端结构域相当。一种纯化的在埋藏侧链中带有替换的突变阻遏蛋白，其氨基末端结构域的热稳定性降低。改变溶剂暴露的野生型侧链的突变可能确定了形成λ阻遏蛋白操纵基因DNA结合表面的残基，而完全或部分埋藏的突变则通过降低蛋白质稳定性发挥其作用。
The DNA binding properties of 52 different single-amino acid substitutions in .lambda. repressor''s amino-terminal domain were characterized. Seven proteins bearing mutations that change solvent-exposed side chains were purified. The amino-terminal domains of these mutant repressors are folded and are comparable to the wild-type amino-terminal domain in thermal stability. A purified mutant repressor bearing a substitution in a buried side chain contains an amino-terminal domain with decreased thermal stability. Mutations that alter solvent-exposed wild-type side chains may define residues that form the operator DNA binding surface of .lambda. repressor whereas completely or partially buried mutations exert their effect by decreasing protein stability.