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.
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
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.
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