FLUOROALUMINATES DO NOT AFFECT THE GUANINE-NUCLEOTIDE BINDING CENTER OF THE PEPTIDE-CHAIN ELONGATION-FACTOR EF-TU

被引：14

作者：

KRAAL, B ^{[1
]}

DEGRAAF, JM ^{[1
]}

MESTERS, JR ^{[1
]}

VANHOOF, PJM ^{[1
]}

JACQUET, E ^{[1
]}

PARMEGGIANI, A ^{[1
]}

机构：

[1] ECOLE POLYTECH,BIOCHIM LAB,F-91128 PALAISEAU,FRANCE

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1990年 / 192卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1990.tb19228.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：

EF‐Tu is often referred to as a model for guanine‐nucleotide‐binding regulatory proteins (G‐proteins), since X‐ray diffraction analysis of its GTP‐binding domain shows a detailed location of the ‘consensus’ amino acid sequences involved in nucleotide binding. Fluoroaluminates are thought to mimick the γ‐phosphate in the GTPase centre on account of their activating effect on a variety of GTP binding proteins. In the case of EF‐Tu, we could find no such effects on the basis of at least three independent functional assays. We did notice, however, complicating interactions between free nucleotides, fluoroaluminates and other ligands. By consequence, if indeed AIF−4 behaves as a γ‐phosphate analogue in G‐proteins, then EF‐Tu must have a different GDP/GTP binding site, despite of the conserved consensus sequences. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：305 / 309

页数：5

共 32 条

[1] ZONE-INTERFERENCE GEL-ELECTROPHORESIS - A NEW METHOD FOR STUDYING WEAK PROTEIN NUCLEIC-ACID COMPLEXES UNDER NATIVE EQUILIBRIUM CONDITIONS [J].