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J. Biol. Chem., Vol. 277, Issue 28, 24995-25000, July 12, 2002
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From the Department of Biochemistry, Duke University Medical
Center, Durham, North Carolina 27710
Escherichia coli MoeA and
MogA are required for molybdenum cofactor biosynthesis and are believed
to function in the addition of molybdenum to the dithiolene of
molybdopterin to form molybdenum cofactor. Here we show that
moeA
Escherichia coli MoeA and MogA
FUNCTION IN METAL INCORPORATION STEP OF MOLYBDENUM COFACTOR
BIOSYNTHESIS*
and mogA cells
are able to synthesize molybdopterin, but both are deficient in
molybdenum incorporation and, as a consequence, are deficient in
the formation of molybdopterin-guanine dinucleotide. Human sulfite
oxidase expressed in E. coli moeA could be
activated in vitro in the presence of MoeA and low
concentrations of molybdate. Sulfite oxidase purified from the
moeA lysate was also activated, although to a
lesser extent than observed in the presence of lysate. MogA was
incapable of activating sulfite oxidase expressed in E. coli
mogA. These results demonstrate that molybdenum
insertion into molybdopterin is required for
molybdopterin-guanine dinucleotide formation, and that MoeA
facilitates molybdenum incorporation at low levels of
molybdate, but MogA has an alternative function, possibly as a carrier for molybdopterin during molybdenum incorporation.
*
This work was supported by National Institutes of Health
Grant GM00091.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 919-681-8845;
Fax: 919-684-8919; E-mail: raj@biochem.duke.edu.
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