ELONGATION FACTOR-TU - A MOLECULAR SWITCH IN PROTEIN-BIOSYNTHESIS

被引:73
作者
WEIJLAND, A [1 ]
HARMARK, K [1 ]
COOL, RH [1 ]
ANBORGH, PH [1 ]
PARMEGGIANI, A [1 ]
机构
[1] ECOLE POLYTECH,BIOCHIM LAB,CNRS,SDI 61840,F-91128 PALAISEAU,FRANCE
关键词
D O I
10.1111/j.1365-2958.1992.tb01516.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
Elongation factor Tu (EF-Tu), the most abundant protein in Escherichia coli, is a guanine nucleotide-binding protein that in the 'on' state acts as a carrier of amino acyl-tRNA to the ribosome. Our knowledge of this essential component of translation has brought substantial progress in the past decade thanks to the co-ordinated application of biochemical, physico-chemical and genetic methods. Crystallographic analysis at 2.6 angstrom resolution and site-directed mutagenesis have revealed structural and functional similarities between the guanine nucleotide-binding domains of EF-Tu and human H-ras p21 protein. The regulation of the expression of the two EF-Tu-encoding genes in E. coli, particularly that of tufB, has been shown to involve diverse mechanisms. Several aspects of the functions of EF-Tu in the elongation cycle have been reinvestigated, leading to new insights. These studies have emphasized the manifold aspects of the mechanisms regulating the activity of EF-Tu in the bacterial cell.
引用
收藏
页码:683 / 688
页数:6
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