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(Received for publication, September 18, 1996, and in revised form, October 30, 1996)
From the Department of Chemistry and Biochemistry, Concordia
University, Montreal, Quebec H3G 1M8, Canada and the
§ Department of Cell and Molecular Biology, Umeå
University, Umeå S-901 87, Sweden
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 active form of the
oxygenase component of phenol hydroxylase.
Volume 272, Number 2,
Issue of January 10, 1997
pp. 945-951
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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