ATPase and GTPase Activities Associated with a Specific 5S RNA-protein Complex

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1973 Oct 1

PMID 4355369

Citations 9

Authors

J R Horne

V A Erdmann

Affiliations

Soon will be listed here.

Abstract

An RNA-protein complex consisting of 5S RNA and two ribosomal proteins, B-L5 and B-L22, was isolated from Bacillus stearothermophilus ribosomes and found to be active in GTP hydrolysis. This activity was not influenced by elongation factor G. Further analysis of this complex showed that it was also able to hydrolyze ATP. Inhibition studies revealed that ATP was a noncompetitive inhibitor of GTP and that GTP was also a noncompetitive inhibitor of ATP, indicating that two different enzymatic sites were involved. Differences in pH optimum and optimal temperature also point to a twosite enzyme complex. Both enzymatic hydrolyses were inhibited by thiostrepton and fusidic acid, which are known inhibitors of protein synthesis.

Citing Articles

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Identification by photo-affinity labeling of the proteins in Escherichia coli ribosomes involved in elongation factor G-dependent GDP binding.

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