FEBS Letters
Volume 514, Issue 1 , Pages 67-69, 6 March 2002

Elongation factor G with effector loop from elongation factor Tu is inactive in translocation

Edited by Lev Kisselev

Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

Received 11 November 2001; received in revised form 19 November 2001; accepted 21 November 2001.

Abstract 

Elongation factors Tu and G (EF-Tu and EF-G) alternately interact with the ribosome during the elongation phase of protein biosynthesis. The function of both factors depends on GTP binding, and the factors are ascribed to a superfamily of G-proteins . All G-proteins contain the effector loop, a structural element that is important for the protein’s interaction with its target molecule. In this study the effector loop of EF-G was replaced by the loop taken from EF-Tu. The EF-G with EF-Tu loop has markedly decreased GTPase activity and did not catalyze translocation. We conclude that these loops are not functionally interchangeable since the factors interact with different states of the ribosome.

Keywords:  Ribosome, Elongation factor G, Translocation, GTP hydrolysis

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PII: S0014-5793(02)02300-1

FEBS Letters
Volume 514, Issue 1 , Pages 67-69, 6 March 2002

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