COMPARISON OF PHOSPHORYLATION OF ELONGATION FACTOR-I FROM DIFFERENT SPECIES BY CASEIN KINASE-II

被引：23

作者：

PALEN, E ^{[1
]}

HUANG, TT ^{[1
]}

TRAUGH, JA ^{[1
]}

机构：

[1] UNIV CALIF RIVERSIDE,DEPT BIOCHEM,RIVERSIDE,CA 92521

来源：

FEBS LETTERS | 1990年 / 274卷 / 1-2期

关键词：

CaScin kinase; Elongation factor; Protein kinase: Protein synthesis: Phosphorylation;

D O I：

10.1016/0014-5793(90)81317-H

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

One subunit of EF-1 or EF-1/βγ from Artemia salina, wheat germ and rabbit reticulocytes is modified by caScin kinase II. The subunit corresponds to the low Mr, subunit of EF-1 (26000-36000) which functions along with a higher Mi subunit (46000-48000). to catalyze the exchange of GDP for GTP on EF-1α. The factor from Artemia and wheat germ is phosphorylated directly on serine by casein kinase II whereas a modulatory compound is required for phosphorylation of EF-1 from reticulocytes. Polylysine increases the rate of phosphorylation of EF-1 from reticulocytes by 24-fold: both serine and threonine arc modified. This suggests that polylysinc may be substituting for a physiological regulatory compound which modulates phosphoryation in vivo. © 1990.

引用

页码：12 / 14

页数：3

共 22 条

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