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Journal of Bacteriology, July 2003, p. 4204-4210, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4204-4210.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Solution Structure of YbcJ from Escherichia coli Reveals a Recently Discovered {alpha}L Motif Involved in RNA Binding

Laurent Volpon,1 Carine Lievre,2 Michael J. Osborne,1 Shaifali Gandhi,2 Pietro Iannuzzi,3 Robert Larocque,3 Miroslaw Cygler,3 Kalle Gehring,1* and Irena Ekiel2,4

Department of Biochemistry, McGill University, Montreal, Quebec, H3G 1Y6,1 NMR Group, Biotechnology Research Institute, National Research Council of Canada,2 Macromolecular Structure Group, Biotechnology Research Institute, Montreal, Quebec, H4P 2R2,3 Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, H3G 1M8, Canada4

Received 7 February 2003/ Accepted 25 April 2003

The structure of the recombinant Escherichia coli protein YbcJ, a representative of a conserved family of bacterial proteins (COG2501), was determined by nuclear magnetic resonance. The fold of YbcJ identified it as a member of the larger family of S4-like RNA binding domains. These domains bind to structured RNA, such as that found in tRNA, rRNA, and a pseudoknot of mRNA. The structure of YbcJ revealed a highly conserved patch of basic residues, comprising amino acids K26, K38, R55, K56, and K59, which likely participate in RNA binding.

* Corresponding author. Mailing address: Dept. of Biochemistry, McGill University, McIntyre Medical Science Building, 3655 Promenade Sir William Osler, Montreal, Quebec, H3G 1Y6, Canada. Phone: (514) 847-9494. Fax: (514) 847-0220. E-mail: kalle.gehring{at}mcgill.ca.

Journal of Bacteriology, July 2003, p. 4204-4210, Vol. 185, No. 14
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.14.4204-4210.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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