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 Previous Article

Journal of Bacteriology, November 2006, p. 7992-7996, Vol. 188, No. 22
0021-9193/06/$08.00+0     doi:10.1128/JB.00959-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Cooperative and Critical Roles for Both G Domains in the GTPase Activity and Cellular Function of Ribosome-Associated Escherichia coli EngA{triangledown}

Amrita Bharat,1 Mengxi Jiang,2 Susan M. Sullivan,2 Janine R. Maddock,2 and Eric D. Brown1*

Antimicrobial Research Centre and Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario L8N 3Z5, Canada,1 Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, Michigan 48109-10482

Received 2 July 2006/ Accepted 29 August 2006

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 an S16A nor an S217A variant of G domain 1 or 2, respectively, was 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 with respect to in vitro GTPase activity. Together, these observations suggest that the G domains have a cooperative function in ribosome stability and/or biogenesis.

* Corresponding author. Mailing address: Antimicrobial Research Centre, Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario L8N 3Z5, Canada. Phone: (905) 525-9140, ext. 22392. Fax: (905) 522-9033. E-mail: ebrown{at}mcmaster.ca.

{triangledown} Published ahead of print on 8 September 2006.

Journal of Bacteriology, November 2006, p. 7992-7996, Vol. 188, No. 22
0021-9193/06/$08.00+0     doi:10.1128/JB.00959-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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