Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids.
Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids.
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同源蛋白的折叠：大肠杆菌、鼠伤寒沙门氏菌和五个种间杂合体色氨酸合酶α亚基折叠机制的保守性。
DOI：
10.1021/bi00402a050
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发表时间：
1988
期刊：
影响因子：
2.9
通讯作者：
Miles,EW
中科院分区：
文献类型：
--
作者：
Stackhouse,TM;Onuffer,JJ;Matthews,CR;Ahmed,SA;Miles,EW
1987年9月21日收到的摘要：比较了尿素诱导的大肠杆菌、鼠伤寒沙门氏菌和5个种间杂种色氨酸合酶a亚基解折叠的平衡和动力学性质，以确定蛋白质折叠在进化中的作用。亲本蛋白质在268个氨基酸的序列中有40个位置不同，杂交体与大肠杆菌a亚基的差异高达15个氨基酸。结果表明，所有蛋白质遵循相同的折叠机制，并且与先前提出的假设一致[Hollecker，M.，& Creighton，T. E.等人（1983）J. Mol. 168，409; Krebs，H.，Schmid，F. X.，& Jaenicke，R.等人（1983）J. Mol. 169，619]，折叠机制在同源蛋白中是保守的。动力学数据的分析表明，亲本蛋白质在氨基折叠单元（残基1-188）上不同的15个位置在折叠中的限速步骤中不起作用，所述限速步骤先前已被鉴定为氨基和羧基折叠单元的缔合[Beasty，AM，Hurle，M. R.，曼兹，J.T.，斯塔克豪斯，T。美国，Onuffer，J. J.，&马修斯，C. R.（1986）Biochemistry 25，2965]，亲本蛋白质在羧基折叠单元上不同的25个位置中的一个或多个，残基189-268，似乎在该相同的限速步骤中发挥作用。
Revised Manuscript Received September 21, 1987 abstract: The equilibrium and kinetic properties for the urea-inducedunfolding of the a subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids were compared to determine the role of protein folding in evolution. The parent proteins differ at 40 positions in the sequence of 268 amino acids, and the hybrids differ by up to 15 amino acids from the Escherichia coli a subunit. The results show that all the proteins follow the same folding mechanismand are consistent with a previously proposed hypothesis [Hollecker, M., & Creighton, T. E.(1983) J. Mol. Biol. 168, 409; Krebs, H., Schmid, F. X., & Jaenicke, R.(1983) J. Mol. Biol. 169, 619] that the folding mechanisms are conserved in homologous proteins. Analysis of the kinetic data suggests that the 15 positions at which the parent proteins differ in the amino folding unit, residues 1-188, donot play a role in a rate-limiting step in folding that has been previously identified as the association of the amino and carboxylfolding units [Beasty, AM, Hurle, M. R., Manz, J. T., Stackhouse, T. S., Onuffer, J. J., & Matthews, C. R.(1986) Biochemistry 25, 2965], One or more of the 25 positions at which the parent proteins differ in the carboxyl foldingunit, residues 189-268, do appear to play a role in this same rate-limiting step.