Open AccessThe myxochelin iron transport regulon of the myxobacterium Stigmatella aurantiaca Sg a15
Author(s) -
Silakowski Barbara,
Kunze Brigitte,
Nordsiek Gabriele,
Blöcker Helmut,
Höfle Gerhard,
Müller Rolf
Publication year - 2000
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.2000.01740.x
Subject(s) - nonribosomal peptide , biochemistry , lysine , gene cluster , siderophore , biology , homology (biology) , amino acid , gene , chemistry , biosynthesis
The biosynthetic gene cluster of the myxochelin‐type iron chelator was cloned from Stigmatella aurantiaca Sg a15 and characterized. This catecholate siderophore was only known from two other myxobacteria. The biosynthetic genes of 2,3‐dihydroxybenzoic acid are located in the cluster ( mxcC – mxcF ). Two molecules of 2,3‐dihydroxybenzoic acid are activated and condensed with lysine in a unique way by a protein homologous to nonribosomal peptide synthetases (MxcG). Inactivation of mxcG, which encodes an adenylation domain for lysine, results in a myxochelin negative mutant unable to grow under iron‐limiting conditions. Growth could be restored by adding Fe 3+ , myxochelin A or B to the medium. Inactivation of mxcD leads to the same phenotype. A new type of reductive release from nonribosomal peptide synthetases of the 2,3‐dihydroxybenzoic acid bis‐amide of lysine from MxcG, catalyzed by a protein domain with homology to NAD(P) binding sites, is discussed. The product of a gene, encoding a protein similar to glutamate‐1‐semialdehyde 2,1‐aminomutases ( mxcL ), is assumed to transaminate the aldehyde that is proposed as an intermediate. Further genes encoding proteins homologous to typical iron utilization and iron uptake polypeptides are reported.