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Escherichia coli elongation-factor-Tu mutants with decreased affinity for aminoacyl-tRNA

Content Provider	Scilit
Author	Andersen, Carsten Wiborg, Ove
Copyright Year	1994
Description	Journal: Journal of Biological Inorganic Chemistry The two evolutionary well-conserved histidine residues, His66 and His118, of Escherichia coli elongation factor Tu have been subjected to mutational analysis. The two histidines have each been replaced by alanines, denoted H66A and H118A, respectively. His118 has also been substituted by glutamate, H118E. The three mutants have been characterized with respect to thermostability, GTPase activity and affinity for aminoacylated tRNA. Most conspicuously, the tRNA affinity is reduced or almost abolished. k-1 for dissociation of the ternary complex increases by factors of 14, 40 and 48 for H66A, H118A and H118E, respectively, when compared to the wild type. The half-lives for the non-enzymic deacylation of aminoacylated tRNA in the ternary complex are 391, 107, 69, 54 and 61 min for wild type, H66A, H118A, H118E and free aminoacylated tRNA, respectively. The Kd is about 20-times higher for H66A compared to wild type. Our results strongly suggest that His66 and His118 play major roles in stabilization of the ternary complex.
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1994.tb18674.x/pdf
Ending Page	744
Page Count	6
Starting Page	739
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1994.tb18674.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	3
Volume Number	220
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1994-03-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Aminoacylated Trna
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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