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J. Bacteriol. doi:10.1128/JB.00959-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

A cooperative and critical role for both G-domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA

Antimicrobial Research Centre and Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario L8N 3Z5, Canada, and Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109-1048, USA

^* To whom correspondence should be addressed. Email: ebrown{at}mcmaster.ca.

	Abstract

To probe the cellular phenotype and biochemical function associated with the G-domains of Escherichia coli EngA (YfgK, Der), mutations were created in the phosphate binding loop of each. Neither S16A nor S217A variants of G-domains 1 and 2, respectively, were able to support growth of an engA conditional null. Polysome profiles of EngA-depleted cells were significantly altered and His₆-EngA was found to cofractionate with the 50S ribosomal subunit. The variants were unable to complement the abnormal polysome profile and were furthermore significantly impacted for in vitro GTPase activity. Together, these observations suggest that the G-domains have a cooperative function in ribosome stability and/or biogenesis.

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