On the role of DmpK, an auxiliary protein associated with multicomponent phenol hydroxylase from Pseudomonas sp. strain CF600.

The Journal of Biological Chemistry
J PowlowskiElisabeth Cadieux

Abstract

DmpK from Pseudomonas sp. strain CF600 represents a group of proteins required by phenol-degrading bacteria that utilize a multicomponent iron-containing phenol hydroxylase. DmpK has been overexpressed in Escherichia coli and purified to homogeneity; it lacks redox cofactors and was found to strongly inhibit phenol hydroxylase in vitro. Chemical cross-linking experiments established that DmpK binds to the two largest subunits of the oxygenase component of the hydroxylase; this may interfere with binding of the hydroxylase activator protein, DmpM, causing inhibition. Since expression of DmpK normally appears to be much lower than that of the components of the oxygenase, inhibition may not occur in vivo. Hence, the interaction between DmpK and the oxygenase manifested in the inhibition and cross-linking results prompted construction of E. coli strains in which the oxygenase component was expressed in the presence and absence of a low molar ratio of DmpK. Active oxygenase was detected only when expressed in the presence of DmpK. Furthermore, inactive oxygenase could be activated in vitro by adding ferrous iron, in a process that was dependent on the presence of DmpK. These results indicate that DmpK plays a role in assembly of the...Continue Reading

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Citations

Apr 30, 2013·Applied Biochemistry and Biotechnology·Shengnan ShiYuanyuan Qu
Dec 16, 1998·Trends in Biochemical Sciences·J Stubbe, P Riggs-Gelasco
Dec 1, 2001·Microbiology and Molecular Biology Reviews : MMBR·E DíazJ L García
Jan 1, 1999·Bioscience, Biotechnology, and Biochemistry·M HorinouchiT Omori
Sep 24, 2013·Journal of Structural Biology·Andrey M GrishinMiroslaw Cygler
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May 20, 2008·Advances in Applied Microbiology·R E ParalesJ L Ditty
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