HOW MANY EF-TU MOLECULES PARTICIPATE IN AMINOACYL-TRANSFER RNA-BINDING

被引：24

作者：

BENSCH, K

PIEPER, U

OTT, G

SCHIRMER, N

SPRINZL, M

PINGOUD, A

机构：

[1] MED HSCH HANNOVER, ZENTRUM BIOCHEM, BIOPHYS CHEM ABT, KONSTANTY GUTSCHOW STR 8, W-3000 HANNOVER 61, GERMANY

[2] UNIV BAYREUTH, BIOCHEM LAB, W-8580 BAYREUTH, GERMANY

来源：

BIOCHIMIE | 1991年 / 73卷 / 7-8期

关键词：

ELONGATION FACTOR-TU; AMINOACYL-TRANSFER RNA; PROTEIN SYNTHESIS;

D O I：

10.1016/0300-9084(91)90146-R

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：

The stoichiometry of the EF-Tu.GTP.aminoacyl-tRNA complex has been re-determined by a variety of methods, viz gel filtrations, fluorescence titrations, as well as hydrolysis and RNase protection experiments. The results of these experiments clearly demonstrate that one aminoacyl-tRNA interacts with only one EF-Tu.GTP molecule, in agreement with the established view and in contrast to the recently published results by Ehrenberg et al [6].

引用

页码：1045 / 1050

页数：6

共 46 条

[1] THE INTERACTION BETWEEN AMINOACYL-TRANSFER RNA AND THE MUTANT ELONGATION FACTOR-TUAR AND FACTOR-TUBO [J].