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J Bacteriol, July 1998, p. 3509-3516, Vol. 180, No. 14
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Glycyl Radical Enzyme TdcE Can Replace Pyruvate Formate-Lyase in Glucose Fermentation

Gary Sawers,1,* Christian Heßlinger,2,dagger Nathalie Muller,2 and Manuela Kaiser2

Nitrogen Fixation Laboratory, John Innes Centre, Norwich, United Kingdom,1 and Lehrstuhl für Mikrobiologie, Universität München, D-80638 Munich, Germany2

Received 5 March 1998/Accepted 8 May 1998

Mutants of Escherichia coli unable to synthesize a functional pyruvate formate-lyase (PFL) are severely impaired in their capacity to grow by glucose fermentation. In a functional complementation assay designed to isolate the pfl gene from Clostridium butyricum, we fortuitously identified a gene that did not encode a PFL but nonetheless was able to complement the phenotypic defects caused by an E. coli pfl mutation. The clostridial gene encoded a basic 14.5-kDa protein (TcbC) which, based on amino acid similarity and analysis of immediately adjacent DNA sequences, was part of a transposase exhibiting extensive similarity to the product of the site-specific transposon Tn554 from Staphylococcus aureus. Our studies revealed that the clostridial TcbC protein activated the transcription of the E. coli tdcABCDEFG operon, which encodes an anaerobic L-threonine-degradative pathway. Normally, anaerobic synthesis of the pathway is optimal when E. coli grows in the absence of catabolite-repressing sugars and in the presence of L-threonine. Although anaerobic control of pathway synthesis was maintained, TcbC alleviated glucose repression. One of the products encoded by the tdc operon, TdcE, has recently been shown to be a 2-keto acid formate-lyase (C. Heßlinger, S. A. Fairhurst, and G. Sawers, Mol. Microbiol. 27:477-492, 1998) that can accept pyruvate as an enzyme substrate. Here we show that TdcE is directly responsible for the restoration of fermentative growth to pfl mutants.

* Corresponding author. Mailing address: Nitrogen Fixation Laboratory, John Innes Centre, Norwich NR4 7UH, United Kingdom. Phone: 44 1603 456900, ext. 2750. Fax: 44 1603 454970. E-mail: gary.sawers{at}bbsrc.ac.uk.

dagger Present address: GSF-Institut für Klinische Molekularbiologie, D-81377 Munich, Germany.

J Bacteriol, July 1998, p. 3509-3516, Vol. 180, No. 14
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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