Characterization and Regulation of the
            <i>gbuA</i>
            Gene, Encoding Guanidinobutyrase in the Arginine Dehydrogenase Pathway of
            <i>Pseudomonas aeruginosa</i>
            PAO1

Nakada, Yuji; Itoh, Yoshifumi

doi:10.1128/jb.184.12.3377-3384.2002

Cited by 29 publications

(40 citation statements)

References 42 publications

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“…Consistent with earlier reports (11,20,32), other known genes of the ADC and ADH pathways were not identified as ArgR-inducible genes by transcriptome analysis. This argues against the function of ArgR in the control of the ADC and ADH pathways for arginine utilization in P. aeruginosa.…”

Section: Discussionsupporting

confidence: 80%

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Transcriptome Analysis of the ArgR Regulon inPseudomonas aeruginosa

Yang

2004

J Bacteriol

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Arginine metabolism in pseudomonads with multiple catabolic pathways for its utilization as carbon and nitrogen sources is of particular interest as the model system to study control of metabolic integration. We performed transcriptome analyses to identify genes controlled by the arginine regulatory protein ArgR and to better understand arginine metabolic pathways of P. aeruginosa. We compared gene expression in wild-type strain PAO1 with that in argR mutant strain PAO501 grown in glutamate minimal medium in the presence and absence of arginine. Ten putative transcriptional units of 28 genes were inducible by ArgR and arginine, including all known ArgR-regulated operons under aerobic conditions. The newly identified genes include the putative adcAB operon, which encodes a catabolic arginine decarboxylase and an antiporter protein, and PA0328, which encodes a hypothetical fusion protein of a peptidase and a type IV autotransporter. Also identified as members of the arginine network are the following solute transport systems: PA1971 (braZ) for branched-chain amino acids permease; PA2042 for a putative sodium:serine symporter; PA3934, which belongs to the family of small oligopeptide transporters; and PA5152-5155, which encodes components of an ABC transporter for a putative opine uptake system. The effect of arginine on the expression of these genes was confirmed by lacZ fusion studies and by DNA binding studies with purified ArgR. Only five transcriptional units of nine genes were qualified as repressible by ArgR and arginine, with three operons (argF, carAB, and argG) in arginine biosynthesis and two operons (gltBD and gdhA) in glutamate biosynthesis. These results indicate that ArgR is important in control of arginine and glutamate metabolism and that arginine and ArgR may have a redundant effect in inducing the uptake systems of certain compounds.Pseudomonas aeruginosa possesses four different catabolic pathways for utilization of arginine (11): the arginine deiminase (ADI) pathway, the arginine succinyltransferase (AST) pathway, the arginine decarboxylase (ADC) pathway, and the arginine dehydrogenase (ADH) pathway (Fig. 1). Under aerobic conditions, Haas and coworkers have established that arginine utilization occurs mainly through the AST pathway, which converts arginine to glutamate (20,43). Recent studies in the laboratories of Lu and Abdelal have shown that the aru operon, which encodes the AST pathway, and the gdhB gene, which encodes a catabolic glutamate dehydrogenase, are inducible by arginine and that this effect is mediated by ArgR (18,24). In P. aeruginosa, ArgR, the arginine-responsive regulator protein, is autoinduced from the aot-argR operon for arginine uptake and regulation (35). The ArgR protein of P. aeruginosa belongs to the AraC/XylS family of transcriptional regulators (7) and is thus quite different in structure and function from the ArgR proteins of enteric bacteria and Bacillus subtilis (3,4,6,23,25), which have a high degree of similarity in their three-dimensional structures and DNA...

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Section: Discussionsupporting

confidence: 80%

“…Exogenous agmatine but not arginine induced these genes (14,29). Very little is known about the enzymes or genes of the ADH pathway; only the gbuA gene and the bifunctional kauB gene have been characterized (32).…”

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confidence: 99%

Transcriptome Analysis of the ArgR Regulon inPseudomonas aeruginosa

Yang

2004

J Bacteriol

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“…Replacing comP in strain NAFM5 with comP : : Spc using a pUC118 derivative carrying a 4?4 kb HindIII fragment containing comP (Tran et al, 2000), which had been inactivated by insertion of the EcoRV-HincII Spc-resistance cassette (see above) at the ClaI site, resulted in strain NAFM65 (comP : : Spc). Southern blotting (Nakada & Itoh, 2002) confirmed that the Spc-resistance cassette and ggt at the target loci were correctly inserted.…”

Section: Construction Of Mutantsmentioning

confidence: 82%

“…The resultant protoplasts were quickly sedimented by centrifugation, and suspended in 10 ml acetate/EDTA buffer (pH 4?8) containing 30 mM sodium acetate, 1 mM EDTA and 10 mM Tris. Thereafter, total RNA was extracted with hot phenol (Nakada & Itoh, 2002). For primer extension analysis, RNA samples (20 mg) were annealed with an oligonucleotide (59-AGCGACTAACAGAACACTAAGCAGAGC-39, complementary to nt 31-58 of ggt) labelled with 32 P at the 59 end by using [c-…”

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confidence: 99%

Characterization of Bacillus subtilis -glutamyltransferase and its involvement in the degradation of capsule poly- -glutamate

Kimura

2004

Microbiology

107

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During early stationary phase, Bacillus subtilis NAFM5 produces capsular poly(c-glutamic acid) (cPGA, 2610 6 Da), which contains D-and L-glutamate, and then degrades it during late stationary phase. The c-glutamyltransferase (EC 2.3.2.2; GGT) of this strain successively hydrolysed cPGA from the amino-terminal end, to yield both D-and L-glutamate. This enzyme was specifically synthesized during the stationary phase through transcriptional activation of the corresponding ggt gene by the ComQXPA quorum-sensing system. A ggt knockout mutant degraded cPGA into 1610 5 Da fragments, but not any further, indicating that the capsule cPGA is first internally degraded by an endo-type of cPGA hydrolase into 1610 5 Da intermediates, then externally into glutamates via GGT. Due to its inability to generate the glutamates from the capsule, the ggt mutant sporulated more frequently than the wild-type strain. The results show that B. subtilis GGT has a powerful exo-c-glutamyl hydrolase activity that participates in capsule cPGA degradation to supply stationary-phase cells with constituent glutamates.

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“…Expression of the aruHI genes encoding the first 2 enzymes of the ATA pathway is controlled by the AruRS 2-component systems (7) in response to L-arginine, and the gbuA gene encoding 4-guanidinobutyrase is controlled by GbuR and 4-guanidinobutyrate (14).…”

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confidence: 99%

Arginine racemization by coupled catabolic and anabolic dehydrogenases

Lu²

2009

Proc. Natl. Acad. Sci. U.S.A.

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amino acid ͉ arginine dehydrogenase ͉ racemase A lthough L-amino acids are the predominant amino acids in protein synthesis, D-amino acids serve as specialized components of many types of machineries in living organisms. In mammals, D-serine and D-aspartate are associated with cell aging and neural signaling (1, 2). In bacteria, some D-amino acids are essential ingredients of cell wall synthesis (3). Endogenous D-amino acids are produced by racemization from the prevalent L-amino acids through the action of racemases. Amino acid racemases are classified into 2 groups: pyridoxal 5Ј phosphate-dependent and phosphate-independent enzymes (4). Completely different reaction mechanisms have been proposed for these 2 groups of enzymes for the spatial rearrangement of ␣-hydrogen in the corresponding amino acids. Nevertheless, racemization of amino acids reported so far is catalyzed by a single enzyme.When provided in excess, some D-amino acids can be used as nutrients to support growth by bacteria. In most cases, D-amino acid oxidase or dehydrogenase catalyzes the oxidative deamination as the first step in catabolism. Pseudomonas aeruginosa, an opportunistic human pathogen with an enormous catabolic capacity, is capable of growing on D-arginine as the sole source of carbon and nitrogen (5). The presence of an inducible D-arginine dehydrogenase activity in this organism was initially reported by Haas and coworkers (6), and 2-ketoarginine derived from this reaction could be converged into the arginine transaminase (ATA) pathway (7,8), 1 of the 4 pathways for L-arginine catabolism in pseudomonads (Fig. 1). In fact, it has been proposed that L-arginine might be converted into D-arginine via racemization (6), reminiscent of L-alanine utilization through a catabolic alanine racemase and D-alanine dehydrogenase in Escherichia coli and many bacteria (9, 10). Existence of an arginine racemase in P. aeruginosa was supported by growth complementation of arginine auxotrophs with D-arginine (6). However, the activity of P. aeruginosa arginine racemase has never been demonstrated in vitro, presumably because of the instant decomposition of both L-and D-arginine in extracts.Under aerobic conditions, L-arginine is preferentially catabolized by the arginine succinyltransferase (AST) pathway, followed by the ATA pathway (7,11). Enzymes of the AST pathway are encoded by the aruCFGDBE operon (12), which is induced by exogenous L-arginine in the presence of a functional arginine regulator, ArgR (13). The ArgR protein belongs to the AraC family of transcriptional regulators. Depending on the location of its binding sites, ArgR serves as a repressor or activator of ArgR regulon in arginine and glutamate metabolism. Thus, when the AST pathway is absent or remains uninduced (e.g., in the argR mutant), the ATA pathway then takes charge as the auxiliary route of L-arginine utilization.

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Characterization and Regulation of the gbuA Gene, Encoding Guanidinobutyrase in the Arginine Dehydrogenase Pathway of Pseudomonas aeruginosa PAO1

Cited by 29 publications

References 42 publications

Transcriptome Analysis of the ArgR Regulon inPseudomonas aeruginosa

Transcriptome Analysis of the ArgR Regulon inPseudomonas aeruginosa

Characterization of Bacillus subtilis -glutamyltransferase and its involvement in the degradation of capsule poly- -glutamate

Arginine racemization by coupled catabolic and anabolic dehydrogenases

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