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Journal of Bacteriology, May 2001, p. 2817-2822, Vol. 183, No. 9
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.9.2817-2822.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Interplay between the Specific Chaperone-Like Proteins HybG and HypC in Maturation of Hydrogenases 1, 2, and 3 from Escherichia coli

Melanie Blokesch, Axel Magalon, and August Böck*

Lehrstuhl für Mikrobiologie der Universität München, D-80638 Munich, Germany

Received 4 December 2000/Accepted 9 February 2001

The hybG gene product from Escherichia coli has been identified as a chaperone-like protein acting in the maturation of hydrogenases 1 and 2. It was shown that HybG forms a complex with the precursor of the large subunit of hydrogenase 2. As with HypC, which is the chaperone-like protein involved in hydrogenase 3 maturation, the N-terminal cysteine residue is crucial for complex formation. Introduction of a deletion into hybG abolished the generation of active hydrogenase 2 but only quantitatively reduced hydrogenase 1 activity since HypC could replace HybG in this function. In contrast, HybG could not take over the role of HypC in a Delta hypC genetic background. Overproduction of HybG, especially of the variants with the replaced N-terminal cysteine residue, strongly interfered with hydrogenase 3 maturation, apparently by titrating some other component(s) of the maturation machinery. The results indicate that the three hydrogenase isoenzymes not only are interacting at the functional level but are also interconnected during the maturation process.

* Corresponding author. Mailing address: Institute of Genetics and Microbiology, University of Munich, Maria-Ward-Strasse 1a, D-80638 Munich, Germany. Phone: 49-89-21806120. Fax: 49-89-21806122. E-mail: august.boeck{at}lrz.uni-muenchen.de.

Journal of Bacteriology, May 2001, p. 2817-2822, Vol. 183, No. 9
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.9.2817-2822.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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