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J Biol Chem, Vol. 275, Issue 7, 4906-4911, February 18, 2000
From the Department of Energy Plant Research Laboratory and
Department of Botany and Plant Pathology, Michigan State University,
East Lansing, Michigan 28824
The cyclic tetrapeptide HC-toxin is an essential
virulence determinant for the plant pathogenic fungus
Cochliobolus carbonum and an inhibitor of histone
deacetylase. The major form of HC-toxin contains the
D-isomers of Ala and Pro. The non-ribosomal peptide synthetase that synthesizes HC-toxin has only one epimerizing domain
for conversion of L-Pro to D-Pro; the source of
D-Ala has remained unknown. Here we present the cloning and
characterization of a new gene involved in HC-toxin biosynthesis,
TOXG. TOXG is present only in HC-toxin-producing
(Tox2+) isolates of C. carbonum. TOXG is able
to support D-Ala-independent growth of a strain of
Escherichia coli defective in D-Ala synthesis. A C. carbonum strain with both of its copies of
TOXG mutated grows normally in culture, and although it no
longer makes the three forms of HC-toxin that contain
D-Ala, it still makes a minor form of HC-toxin that
contains Gly in place of D-Ala. The addition of
D-Ala to the culture medium restores production of the
D-Ala-containing forms of HC-toxin by the toxG
mutant. The toxG mutant has only partially reduced
virulence. It is concluded that TOXG encodes an alanine
racemase whose function is to synthesize D-Ala for incorporation into HC-toxin.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF169478.
A Eukaryotic Alanine Racemase Gene Involved in Cyclic Peptide
Biosynthesis*
*
This research was supported by grants from the United States
Department of Energy, Division of Energy Biosciences and the United
States National Institutes of Health.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.: 517-353-4885;
Fax: 517-353-9168; E-mail: walton@pilot.msu.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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