PURIFICATION AND CHARACTERIZATION OF A PROTEIN FACTOR THAT REVERSES THE INHIBITION OF PROTEIN-SYNTHESIS BY THE HEME-REGULATED TRANSLATIONAL INHIBITOR IN RABBIT RETICULOCYTE LYSATES

被引：97

作者：

AMESZ, H

GOUMANS, H

HAUBRICHMORREE, T

VOORMA, HO

BENNE, R

机构：

[1] Vakgroep Moleculaire Celbiologie, Rijksuniversiteit te Utrecht, Universiteit's Centrum ‘De Uithof’, Utrecht, 3584 CH

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 98卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1979.tb13212.x

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：

We have purified and partially characterized a supernatant factor which reverses the effect of the heme‐regulated translational inhibitor on protein synthesis in rabbit reticulocyte lysates. The anti‐inhibitor restores protein synthesis activity in heme‐deficient lysates (and in lysates to which the inhibitor has been added) to the level observed in the presence of heme. The factor has no effect on the phosphorylation of eIF‐2 by the inhibitor nor on any reaction carried out with purified initiation factors. The anti‐inhibitor probably consists of three subunits with molecular weights of 81000, 60000 and 41000. The factor is isolated from the postribosomal supernatant of rabbit reticulocytes both free and complexed to eIF‐2. A possible mechanism of action is discussed. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：513 / 520

页数：8

共 40 条

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