HOW MANY EF-TU MOLECULES PARTICIPATE IN AMINOACYL-TRANSFER-RNA BINDING AND PEPTIDE-BOND FORMATION IN ESCHERICHIA-COLI TRANSLATION

被引：85

作者：

EHRENBERG, M

ROJAS, AM

WEISER, J

KURLAND, CG

机构：

[1] Department of Molecular Biology, BMC, S-751 24 Uppsala

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1990年 / 211卷 / 04期

关键词：

D O I：

10.1016/0022-2836(90)90074-V

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 observed that two EF-Tu · GTP cycles are required to make one peptide bond during steady-state translation in an accurate and fast poly(U) translation system prepared from Escherichia coli. We have also found that there are two complexes of EF-Tu · GTP bound to one molecule of aminoacyl-tRNA under our experimental conditions. We suggest, on the basis of these data, that aminoacyl-tRNA enters the ribosomal A-site in a pentameric complex together with two EF-Tu and two GTP molecules. When the tRNA is delivered to the ribosome two GTP molecules are hydrolyzed. It is possible that the functional role of such an EF-Tu dimer is related to the function of the two L7/L12 dimers in the large ribosomal subunit. © 1990.

引用

页码：739 / 749

页数：11

共 51 条

[1] DIRECT DETERMINATION OF THE ASSOCIATION CONSTANT BETWEEN ELONGATION-FACTOR TU.GTP AND AMINOACYL-TRANSFER RNA USING FLUORESCENCE [J].