N端甲硫氨酸加工
N-Terminal Methionine Processing.
作者信息
Wingfield Paul T
机构信息
Protein Expression Laboratory, NIAMS/NIH, Bethesda, Maryland.
出版信息
Curr Protoc Protein Sci. 2017 Apr 3;88:6.14.1-6.14.3. doi: 10.1002/cpps.29.
Abstract
Protein synthesis is initiated by methionine in eukaryotes and by formylmethionine in prokaryotes. N-terminal methionine can be co-translationally cleaved by the enzyme methionine aminopeptidase (MAP). When recombinant proteins are expressed in bacterial and mammalian expression systems, there is a simple universal rule that predicts whether the initiating methionine will be processed by MAP based on the size of the residue adjacent (penultimate) to the N-methionine. In general, if the side chains of the penultimate residues have a radius of gyration of 1.29 Å or less, methionine is cleaved. © 2017 by John Wiley & Sons, Inc.
摘要
在真核生物中，蛋白质合成由甲硫氨酸起始，而在原核生物中则由甲酰甲硫氨酸起始。N 端甲硫氨酸可被甲硫氨酸氨肽酶（MAP）共翻译切割。当重组蛋白在细菌和哺乳动物表达系统中表达时，有一个简单通用的规则可根据紧邻 N - 甲硫氨酸的残基（倒数第二个）的大小来预测起始甲硫氨酸是否会被 MAP 加工。一般来说，如果倒数第二个残基的侧链回转半径为 1.29 Å 或更小，甲硫氨酸就会被切割。© 2017 约翰威立国际出版公司。
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