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Journal of Bacteriology, January 2008, p. 434-437, Vol. 190, No. 1
0021-9193/08/$08.00+0     doi:10.1128/JB.01058-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

A Novel Peroxiredoxin Activity Is Located within the C-Terminal End of Rhodospirillum rubrum Adenylyltransferase{triangledown}

Anders Jonsson,{dagger} Pedro Filipe Teixeira,{dagger} and Stefan Nordlund*

Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden

Received 5 July 2007/ Accepted 11 October 2007

Adenylyltransferase (GlnE) catalyzes the reversible adenylylation of glutamine synthetase. In this report we present, for the first time, evidence for a peroxiredoxin activity of Rhodospirillum rubrum GlnE, through the carboxyl-terminal AhpC/thiol-specific antioxidant (TSA) domain. The combination of GlnE and AhpC/TSA domains within the same polypeptide constitutes a unique domain architecture that has not previously been identified among proteobacteria.

* Corresponding author. Mailing address: Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden. Phone: 46 8 16 2932. Fax: 46 8 15 7794. E-mail: stefan{at}dbb.su.se

{triangledown} Published ahead of print on 19 October 2007.

{dagger} A.J. and P.F.T. contributed equally to this work.

Journal of Bacteriology, January 2008, p. 434-437, Vol. 190, No. 1
0021-9193/08/$08.00+0     doi:10.1128/JB.01058-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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