Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes

Rowland, Belinda; Grossman, Trudy H.; Osburne, Marcia S.; Taber, Harry

doi:10.1016/0378-1119(96)00349-6

Cited by 55 publications

(52 citation statements)

References 18 publications

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“…ORF 8 encodes a protein highly similar (Table 3) to DhbF from B. subtilis (Rowland et al, 1996), which is highly related to the E. coli EntF protein that participates in the final stages of enterobactin biosynthesis (Rusnak et al, 1991). RT-PCR experiments proved that this gene is part of a bicistronic message (Fig.…”

Section: Nucleotide Analysis Of Siderophore Biosynthetic and Utilizatmentioning

confidence: 96%

“…1) abolished the complementing activity of pMU85 (Table 2), which confirms the role of this A. baumannii gene in this heterologous system. The dhbA gene encodes a predicted protein with the highest similarity (Table 3) to the B. subtilis DhbA (Rowland et al, 1996), which displays the signature pattern for proteins belonging to the short-chain dehydrogenase/reductase family. ORF 5 encodes a predicted protein highly related to EntC-like proteins, displaying the highest similarity to DhbC from B. subtilis (Rowland et al, 1996) (Table 3).…”

Section: Nucleotide Analysis Of Siderophore Biosynthetic and Utilizatmentioning

confidence: 99%

“…Next is ORF 4 (Fig. 1), which encodes a protein highly similar to several bacterial proteins involved in the activation of DHBA, particularly to DhbE from B. subtilis (Rowland et al, 1996) (Table 3). The restoration of the iron-uptake proficiency and enterobactin production by the presence of pMU73 in the E. coli AN93 entE mutant supports the role of this A. baumannii 8399 siderophore biosynthetic gene.…”

Section: Nucleotide Analysis Of Siderophore Biosynthetic and Utilizatmentioning

confidence: 99%

“…The restoration of the iron-uptake proficiency and enterobactin production by the presence of pMU73 in the E. coli AN93 entE mutant supports the role of this A. baumannii 8399 siderophore biosynthetic gene. ORF 3, the last component of the A. baumannii 8399 dhbACEB polycistronic locus, encodes a protein related to several EntB-like bacterial proteins, with the highest similarity (Table 3) to the DhbB from B. subtilis (Rowland et al, 1996). The amino end of this predicted protein contains the domain found in other isochorismatases, while its carboxyl end includes an acyl carrier protein phosphopantetheinyl (ACP) domain.…”

Section: Nucleotide Analysis Of Siderophore Biosynthetic and Utilizatmentioning

confidence: 99%

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Genetic organization of an Acinetobacter baumannii chromosomal region harbouring genes related to siderophore biosynthesis and transport

et al. 2003

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The Acinetobacter baumannii 8399 clinical isolate secretes dihydroxybenzoic acid (DHBA) and a high-affinity catechol siderophore, which is different from other bacterial iron chelators already characterized. Complementation assays with enterobactin-deficient Escherichia coli strains led to the isolation of a cosmid clone containing A. baumannii 8399 genes required for the biosynthesis and activation of DHBA. Accordingly, the cloned fragment harbours a dhbACEB polycistronic operon encoding predicted proteins highly similar to several bacterial proteins required for DHBA biosynthesis from chorismic acid. Genes encoding deduced proteins related to the E. coli Fes and the Bacillus subtilis DhbF proteins, and a putative Yersinia pestis phosphopantetheinyl transferase, all of them involved in the assembly and utilization of catechol siderophores in other bacteria, were found next to the dhbACEB locus. This A. baumannii 8399 gene cluster also contained the om73, p45 and p114 predicted genes encoding proteins potentially involved in transport of ferric siderophore complexes. The deduced products of the p114 and p45 genes are putative membrane proteins that belong to the RND and MFS efflux pump proteins, respectively. Interestingly, P45 is highly related to the E. coli P43 (EntS) protein that participates in the secretion of enterobactin. Although P114 is similar to other bacterial efflux pump proteins involved in antibiotic resistance, its genetic arrangement within this A. baumannii 8399 locus is different from that described in other bacteria. The product of om73 is a Fur-and iron-regulated surface-exposed outer-membrane protein. These characteristics together with the presence of a predicted TonB box and its high similarity to other siderophore receptors indicate that OM73 plays such a role in A. baumannii 8399. The 184 nt om73-p114 intergenic region contains promoter elements that could drive the expression of these divergently transcribed genes, all of which are in close proximity to almost perfect Fur boxes. This arrangement explains the iron-and Fur-regulated expression of om73, and provides strong evidence for a similar regulation for the expression of p114. INTRODUCTIONBacteria survive and multiply under iron-limiting conditions, such as those found in natural and medical environments, by expressing active systems that gather this micronutrient, which is essential for most micro-organisms with some exceptions such as lactobacilli. Some systems involve the secretion of low-molecular-mass ferric-binding compounds called siderophores, which can be classified into different categories based on their chemical structure (Neilands, 1981(Neilands, , 1995. Many of these high-affinity ironchelating molecules contain catecholate groups that are part of the iron-binding site. Enterobactin, the prototype catechol siderophore produced by Escherichia coli, is a cyclic trimer of 2,3-dihydroxybenzoyl-L-serine (O'Brien & Gibson, 1970;Walsh et al., 1990). In contrast, siderophores such as vibriobactin and anguibactin, produced by...

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Section: Nucleotide Analysis Of Siderophore Biosynthetic and Utilizatmentioning

confidence: 96%

Section: Nucleotide Analysis Of Siderophore Biosynthetic and Utilizatmentioning

confidence: 99%

Section: Nucleotide Analysis Of Siderophore Biosynthetic and Utilizatmentioning

confidence: 99%

Section: Nucleotide Analysis Of Siderophore Biosynthetic and Utilizatmentioning

confidence: 99%

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Genetic organization of an Acinetobacter baumannii chromosomal region harbouring genes related to siderophore biosynthesis and transport

et al. 2003

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“…During pyochelin biosynthesis in P. aeruginosa, the pchD product adenylates salicylic acid, and the activated salicylyl group remains bound to the enzyme for transfer to a thiol in the peptide carrier domain of peptide synthetase PchE (Quadri et al, 1999). Likewise in B. subtilis, DhbE adenylates 2,3-dihydroxybenzoic acid for eventual transfer to glycine (Rowland et al, 1996). The close sequence similarity between CmlK, PchD and DhbE implies that the gene product adenylates aromatic carboxylic acids rather than amino acids.…”

Section: Function Of Cmlkmentioning

confidence: 99%

Biosynthesis of the dichloroacetyl component of chloramphenicol in Streptomyces venezuelae ISP5230: genes required for halogenation

2004

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Five ORFs were detected in a fragment from the Streptomyces venezuelae ISP5230 genomic DNA library by hybridization with a PCR product amplified from primers representing a consensus of known halogenase sequences. Sequencing and functional analyses demonstrated that ORFs 11 and 12 (but not ORFs 13-15) extended the partially characterized gene cluster for chloramphenicol (Cm) biosynthesis in the chromosome. Disruption of ORF11 (cmlK) or ORF12 (cmlS) and conjugal transfer of the insertionally inactivated genes to S. venezuelae gave mutant strains VS1111 and VS1112, each producing a similar series of Cm analogues in which unhalogenated acyl groups replaced the dichloroacetyl substituent of Cm. 1 H-NMR established that the principal metabolite in the disrupted strains was the a-N-propionyl analogue. The sequence of CmlK implicated the protein in adenylation, and involvement in halogenation was inferred from biosynthesis of analogues by the cmlK-disrupted mutant. A role in generating the dichloroacetyl substituent was supported by partial restoration of Cm biosynthesis when a cloned copy of cmlK was introduced in trans into VS1111. Complementation of the mutant also indicated that inactivation of cmlK rather than a polar effect of the disruption on cmlS expression had interfered with dichloroacetyl biosynthesis. The deduced CmlS sequence resembled sequences of FADH 2 -dependent halogenases. Conjugal transfer of cmlK or cmlS into S. venezuelae cml-2, a chlorination-deficient strain with a mutation mapped genetically to the Cm biosynthesis gene cluster, did not complement the cml-2 lesion, suggesting that one or more genes in addition to cmlK and cmlS is needed to assemble the dichloroacetyl substituent. Insertional inactivation of ORF13 did not affect Cm production, and the products of ORF14 and ORF15 matched Streptomyces coelicolor A3(2) proteins lacking plausible functions in Cm biosynthesis. Thus cmlS appears to mark the downstream end of the gene cluster.

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Iron Acquisition by Bacillus anthracis

Pishchany

Skaar

2010

Bacillus Anthracis and Anthrax

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Sequence and genetic organization of a Bacillus subtilis operon encoding 2,3-dihydroxybenzoate biosynthetic enzymes

Cited by 55 publications

References 18 publications

Genetic organization of an Acinetobacter baumannii chromosomal region harbouring genes related to siderophore biosynthesis and transport

Genetic organization of an Acinetobacter baumannii chromosomal region harbouring genes related to siderophore biosynthesis and transport

Biosynthesis of the dichloroacetyl component of chloramphenicol in Streptomyces venezuelae ISP5230: genes required for halogenation

Iron Acquisition by Bacillus anthracis

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