Arginine Hydroxamate-resistant Mutants of Bacillus subtilis with Altered Control of Arginine Metabolism

Harwood, Colin R.; Baumberg, Simon

doi:10.1099/00221287-100-1-177

Cited by 52 publications

(42 citation statements)

References 9 publications

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“…This finding suggests that sufficient NH4' is produced by the catabolism of urea and asparagine to repress the synthesis of their degradative enzymes. The elevation of urease synthesis in arginine-grown cells suggests that this enzyme may be involved in the degradation of urea derived from arginine (10) and may therefore be induced by arginine.…”

Section: Discussionmentioning

confidence: 99%

Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis

Atkinson

Fisher

1991

J Bacteriol

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The levels of urease and asparaginase were elevated 25-and 20-fold, respectively, in extracts of Bacillus subtilis cells grown in medium containing nitrogen sources that are poor sources of ammonium (NH4+) compared with the levels seen in extracts of cells grown in medium containing nitrogen sources that are good sources of NH4+. To determine whether a collection of genes whose expression responds to nitrogen availability could be isolated, a library of Tn917-lacZ insertions was screened for nitrogen-regulated ,1-galactosidase expression. Two fusion strains were identified. I8-Galactosidase expression was 26-and 4,000-fold higher, respectively, in the nrg-21::Tn917-lacZ and the nrg-29::Tn917-lacZ insertion strains during NH4+-restricted growth than during growth on nitrogen sources that are good sources of NH4+. PBS1 transduction analysis showed that the nrg-21::Tn917-lacZ insertion mapped between gutB and purB and that the nrg-29::Tn917-lacZ insertion mapped between degSU and spoIID. The repression of expression of these four gene products during growth on good sources of NH4+ required the wild-type glutamine synthetase protein but not the glutamine synthetase regulatory protein, GlnR.

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Section: Discussionmentioning

confidence: 99%

Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis

Atkinson

Fisher

1991

J Bacteriol

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“…Ornithine transcarbamoyltransferase (OCTase) assays A modification of the method of Harwood and Baumberg (1977), in which the accumulation of citrulline is measured spectrophotometrically, was used .…”

Section: Microbiological and Molecular Biological Techniquesmentioning

confidence: 99%

DNA binding of Escherichia coli arginine repressor mutants altered in oligomeric state

Chen

Merican

Sherratt

1997

Molecular Microbiology

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SummaryThe Escherichia coli arginine repressor (ArgR) controls expression of the arginine biosynthetic genes and acts as an accessory protein in Xer site-specific recombination at cer and related plasmid recombination sites. The hexameric wild-type protein shows L-arginine-dependent DNA binding. In this work, ArgR mutants that are defective in trimer-trimer interactions and bind DNA as trimers in an L-arginine-independent manner are isolated and characterized. Whereas the wild-type ArgR hexamer exhibits high-affinity binding to two repeated ARG boxes separated by 3 bp (each ARG box containing two identical dyad symmetrical 9 bp half-sites), the trimeric mutants bind to and footprint three adjacent half-sites of this 'idealized' substrate. Trimeric ArgR is impaired in its ability to repress the arginine biosynthetic genes and in Xer site-specific recombination. In the absence of L-arginine, residual wild-type ArgR-binding occurs as trimers. The binding of an N-terminal 77-amino-acid DNA-binding domain to idealized ARG boxes is also characterized.

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“…AhrC was ®rst characterized in mutants resistant to the arginine analogue arginine hydroxymate (Harwood & Baumberg, 1977;Mountain & Baumberg, 1980;Smith et al, 1986a,b). Mutants mapping to ahrC, one of four arginine hydroxymate resistant loci, showed simultaneous loss of repression of the biosynthetic genes and activation of the catabolic genes, suggesting the ahrC gene product was a direct regulatory link between the pathways.…”

Section: Introductionmentioning

confidence: 99%

The structure of AhrC, the arginine repressor/activator protein fromBacillus subtilis

Dennis

Glykos

Parsons

et al. 2002

Acta Crystallogr D Biol Cryst

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research papers 422 Dennis et al. AhrC Acta Cryst. (2002). D58, 421±430 pseudo-palindromic ARG boxes which are the binding sites for the E. coli arginine repressor ArgR (ArgREc; Glansdorff, 1987; Smith et al., 1989). Examination of the argC promoter and gene using DNase I and hydroxyl radical footprinting revealed two AhrC-binding sites, which were named argC 01 and argC 02. The higher af®nity binding site, argC 01 , contains two ARG boxes separated by 11 bp and lies within the argC promoter, whilst the lower af®nity site, argC 02 , contains a single ARG box and is located within the argC structural gene (Czaplewski et al., 1992). The argG promoter contains two ARG boxes, separated by 2 bp, upstream of the transcription start site (Miller, 1997). The B. subtilis arginine catabolic pathway contains six enzymes encoded by genes within the two clusters rocABC and rocDEF. AhrC has been shown to interact in an l-arginine-dependent manner with operators within the promoter regions of rocA and rocD. Each of these operators consists of a single ARG box which is located directly adjacent to the transcription start site (Calogero et al., 1994; Klingel et al., 1995; Gardan et al., 1995; Miller et al., 1997). The af®nity of AhrC for the catabolic operators is 10-to 20-fold less than for the biosynthetic gene promoters (Miller et al., 1997), a ®nding consistent with the notion of cooperative binding of AhrC to the tandem repeats of ARG boxes within the upstream regulatory regions of argC and argG. The mechanism by which AhrC activates transcription from rocA and rocD remains unclear, although AhrC binding has been shown to increase the natural bend of the rocA promoter (Miller et al., 1997), which may facilitate interactions with RNA polymerase. Arginine-regulatory proteins, which are usually called ArgR in organisms other than B. subtilis, have been identi®ed in E. coli (Lim et al., 1987), B. stearothermophilus (Dion et al., 1997) and Salmonella typhimurium (Lu et al., 1992). These proteins have been biochemically characterized and shown to act as repressors of arginine biosynthesis in their respective hosts, although any roles in the activation of arginine catabolism remain to be con®rmed experimentally. Sequences are also known for probable AhrC/ArgR homologues from Clostridium perfringens (Ohtani et al., 1997), Haemophilus in¯uenzae (Fleischmann et al., 1995), Mycobacterium tuberculosis (Cole et al., 1998), Streptomyces clavuligerus (Rodriguez-Garcia et al., 1997) and Streptococcus pneumoniae (Priebe et al., 1988). The best characterized of the AhrC homologues is ArgR of E. coli (ArgREc; Lim et al., 1987; Maas, 1994). AhrC and ArgREc share 27% identity (North et al., 1989) and can crossfunction to some extent in vivo. AhrC can repress E. coli arginine genes and complement for ArgR as an essential accessory protein in the resolution of plasmid ColE1 multimers (Stirling et al., 1988); however, ArgR cannot repress the B. subtilis argC promoter (Smith et al., 1989). AhrC and ArgR both require the binding of l-arginine for hig...

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Arginine Hydroxamate-resistant Mutants of Bacillus subtilis with Altered Control of Arginine Metabolism

Cited by 52 publications

References 9 publications

Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis

Identification of genes and gene products whose expression is activated during nitrogen-limited growth in Bacillus subtilis

DNA binding of Escherichia coli arginine repressor mutants altered in oligomeric state

The structure of AhrC, the arginine repressor/activator protein fromBacillus subtilis

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