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J. Biol. Chem., Vol. 275, Issue 37, 28802-28809, September 15, 2000
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From the Department of Biochemistry, Queen's University,
Kingston, Ontario K7L 3N6, Canada
A search of the Bacillus subtilis
genome identifies a potential homolog, ypmQ, of the inner
mitochondrial membrane protein Sco1 from yeast. Sco1 has been found to
aid the delivery of copper to cytochrome c oxidase.
B. subtilis expresses two members of the cytochrome oxidase
family, a cytochrome c oxidase that has two copper centers,
CuA and CuB, and a menaquinol oxidase that has
only CuB. Deletion of ypmQ in B. subtilis depresses expression of cytochrome c oxidase
but not menaquinol oxidase. Levels of cytochrome c oxidase
recover when copper is added to the growth medium of the
Characterization of YpmQ, an Accessory Protein Required for the
Expression of Cytochrome c Oxidase in Bacillus
subtilis*
ypmQ strain or when ypmQ is expressed from a
plasmid. Neither treatment affects the amount or activity of menaquinol oxidase. YpmQ in which two conserved cysteines are replaced by serines
and a conserved histidine is replaced by alanine do not complement the
deletion of ypmQ even though these mutant forms are found
in the membrane extract at a level similar to the wild type protein. We
propose that the two cysteines and the histidine are critical for the
function of YpmQ and suggest they are involved in copper exchange
between YpmQ and the CuA site of cytochrome c oxidase.
*
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.: 613-533-6375;
Fax: 613-533-2497; E-mail: hillb@post.queensu.ca.
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