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J. Biol. Chem., Vol. 276, Issue 40, 37289-37298, October 5, 2001
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From Philipps-Universität Marburg, Fachbereich
Chemie/Biochemie, Hans-Meerwein-Str., Marburg D-35032, Germany
4'-Phosphopantetheine transferases (PPTases)
transfer the 4'-phosphopantetheine moiety of coenzyme A onto a
conserved serine residue of acyl carrier proteins (ACPs) of fatty acid
and polyketide synthases as well as peptidyl carrier proteins (PCPs) of
nonribosomal peptide synthetases. This posttranslational modification
converts ACPs and PCPs from their inactive apo into the active holo
form. We have investigated the 4'-phosphopantetheinylation reaction in
Bacillus subtilis, an organism containing in total 43 ACPs and PCPs but only two PPTases, the acyl carrier protein synthase AcpS
of primary metabolism and Sfp, a PPTase of secondary metabolism associated with the nonribosomal peptide synthetase for the peptide antibiotic surfactin. We identified and cloned ydcB
encoding AcpS from B. subtilis, which complemented an
Escherichia coli acps disruption mutant. B. subtilis AcpS and its substrate ACP were biochemically
characterized. AcpS also modified the D-alanyl carrier protein but failed to recognize PCP and an acyl carrier protein of secondary metabolism discovered in this study, designated AcpK, that
was not identified by the Bacillus genome project. On the other hand, Sfp was able to modify in vitro all acyl
carrier proteins tested. We thereby extend the reported broad
specificity of this enzyme to the homologous ACP. This in
vitro cross-interaction between primary and secondary metabolism
was confirmed under physiological in vivo conditions by the
construction of a ydcB deletion in a B. subtilis
sfp+ strain. The genes coding for Sfp and its homolog
Gsp from Bacillus brevis could also complement the E. coli acps disruption. These results call into question the
essential role of AcpS in strains that contain a Sfp-like PPTase and
consequently the suitability of AcpS as a microbial target in such strains.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF260727.
4'-Phosphopantetheine Transfer in Primary and Secondary
Metabolism of Bacillus subtilis*
§,
*
Work in the laboratory of M. A. M. was supported by
Deutsche Forschungsgemeinschaft and Fonds der Chemischen Industrie.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.
A Ph.D. fellow of Stiftung Stipendien-Fonds des Verbandes der
Chemischen Industrie.
§
These authors contributed equally to this work.
¶
To whom correspondence should be addressed:
Philipps-Universität Marburg, Fachbereich Chemie/Biochemie,
Hans-Meerwein-Str., D-35032 Marburg, Germany. Tel.:
49-6421-2825722; Fax: 49-6421-2822191; E-mail:
Marahiel@chemie.uni-marburg.de.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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