The role of the bacitracin ABC transporter in bacitracin resistance and collateral detergent sensitivity

Podlesek, Zdravko; Comino, Aleksandra; Herzog-Velikonja, Blagajana; Grabnar, M.

doi:10.1111/j.1574-6968.2000.tb09176.x

Cited by 38 publications

(22 citation statements)

References 12 publications

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“…Bacitracin inhibits the biosynthesis of the bacterial cell wall by inhibiting dephosphorylation of C 55 -isoprenyl pyrophosphate (35,36). Like LanFEG, the bacitracin resistance ABC transporter was presumed to transport bacitracin from the membrane (28,29). To investigate the function of the E loop, we constructed 2 E-loop mutants of NukF, namely, E85Q and E85A, corresponding to replacement with glutamine and alanine, respectively.…”

Section: Resultsmentioning

confidence: 99%

Functional Significance of the E Loop, a Novel Motif Conserved in the Lantibiotic Immunity ATP-Binding Cassette Transport Systems

Okuda¹,

Yanagihara²,

Sugayama³

et al. 2010

J Bacteriol

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Lantibiotics are peptide-derived antibacterial substances produced by some Gram-positive bacteria and characterized by the presence of unusual amino acids, like lanthionines and dehydrated amino acids. Because lantibiotic producers may be attacked by self-produced lantibiotics, they express immunity proteins on the cytoplasmic membrane. An ATP-binding cassette (ABC) transport system mediated by the LanFEG protein complex is a major system in lantibiotic immunity. Multiple-sequence alignment analysis revealed that LanF proteins contain the E loop, a variant of the Q loop, which is a well-conserved motif in the nucleotide-binding domains (NBDs) of general ABC transporters. To elucidate E loop function, we introduced a mutation in the NukF protein, which is involved in the nukacin-ISK-1 immunity system. Amino acid replacement of glutamic acid in the E loop with glutamine (E85Q) resulted in slight decreases in the immunity level and transport activity. Additionally, the E85A mutation severely impaired the immunity level and transport activity. On the other hand, ATPase activities of purified E85Q and E85A mutants were almost similar to that of the wild type. These results suggested that the E loop found in ABC transporters involved in lantibiotic immunity plays a significant role in the function of these transporters, especially in the structural change of transmembrane domains.

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Section: Resultsmentioning

confidence: 99%

Functional Significance of the E Loop, a Novel Motif Conserved in the Lantibiotic Immunity ATP-Binding Cassette Transport Systems

Okuda¹,

Yanagihara²,

Sugayama³

et al. 2010

J Bacteriol

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“…The BcrABC transporter provides immunity to the bacitracin-producing strain B. licheniformis. In this system, the BcrB and BcrC proteins form a transmembrane channel, while two BcrA proteins function as ATPases to provide energy for transport (19). Recently, the two-component regulatory system BacRS was identified as a regulator of bcrABC expression (18).…”

mentioning

confidence: 99%

Regulation of the Bacillus subtilis bcrC Bacitracin Resistance Gene by Two Extracytoplasmic Function σ Factors

2002

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Bacitracin resistance is normally conferred by either of two major mechanisms, the BcrABC transporter, which pumps out bacitracin, or BacA, an undecaprenol kinase that provides C 55 -isoprenyl phosphate by de novo synthesis. We demonstrate that the Bacillus subtilis bcrC (ywoA) gene, encoding a putative bacitracin transport permease, is an important bacitracin resistance determinant. A bcrC mutant strain had an eightfoldhigher sensitivity to bacitracin. Expression of bcrC initiated from a single promoter site that could be recognized by either of two extracytoplasmic function (ECF) factors, X or M . Bacitracin induced expression of bcrC, and this induction was dependent on M but not on X . Under inducing conditions, expression was primarily dependent on M . As a consequence, a sigM mutant was fourfold more sensitive to bacitracin, while the sigX mutant was only slightly sensitive. A sigX sigM double mutant was similar to a bcrC mutant in sensitivity. These results support the suggestion that one function of B. subtilis ECF factors is to coordinate antibiotic stress responses.

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“…UPP phosphatases of the PAP2 family, such as BcrC in Bacillus subtilis (formerly YwoA) (3), are found in some gram-positive bacteria, in which they compete with bacitracin for UPP, thus conferring a certain level of protection on the cells (4,23). The bacitracin producer Bacillus licheniformis ATCC 10716 possess two PAP2 family members, BcrC and a BcrC-like protein (YP_080959) (21,27,38). However, in addition to the UPP phosphatases, some gram-positive bacteria also possess an ABC transporter(s), which is an even more efficient bacitracin protection system.…”

mentioning

confidence: 99%

Resistance to Bacitracin in Bacillus subtilis : Unexpected Requirement of the BceAB ABC Transporter in the Control of Expression of Its Own Structural Genes

et al. 2007

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The Bacillus subtilis BceAB ABC transporter involved in a defense mechanism against bacitracin is composed of a membrane-spanning domain and a nucleotide-binding domain. Induction of the structural bceAB genes requires the BceR response regulator and the BceS histidine kinase of a signal transduction system. However, despite the presence of such a transduction system and of bacitracin, no transcription from an unaltered bceA promoter is observed in cells lacking the BceAB transporter. Expression in trans of the BceAB transporter in these bceAB cells restores the transcription from the bceA promoter. Cells possessing a mutated nucleotidebinding domain of the transporter are also no longer able to trigger transcription from the bceA promoter in the presence of bacitracin, although the mutated ABC transporter is still bound to the membrane. In these cells, expression of the bceA promoter can no longer be detected, indicating that the ABC transporter not only must be present in the cell membrane, but also must be expressed in a native form for the induction of the bceAB genes. Several hypotheses are discussed to explain the simultaneous need for bacitracin, a native signal transduction system, and an active BceAB ABC transporter to trigger transcription from the bceA promoter.

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The role of the bacitracin ABC transporter in bacitracin resistance and collateral detergent sensitivity

Cited by 38 publications

References 12 publications

Functional Significance of the E Loop, a Novel Motif Conserved in the Lantibiotic Immunity ATP-Binding Cassette Transport Systems

Functional Significance of the E Loop, a Novel Motif Conserved in the Lantibiotic Immunity ATP-Binding Cassette Transport Systems

Regulation of the Bacillus subtilis bcrC Bacitracin Resistance Gene by Two Extracytoplasmic Function σ Factors

Resistance to Bacitracin in Bacillus subtilis : Unexpected Requirement of the BceAB ABC Transporter in the Control of Expression of Its Own Structural Genes

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