Purification of histidase from Streptomyces griseus and nucleotide sequence of the hutH structural gene

Wu, Pen-Chaur; Kroening, T A; White, Peter J; Kendrick, Kathleen E.

doi:10.1128/jb.174.5.1647-1655.1992

Cited by 26 publications

(14 citation statements)

References 40 publications

(43 reference statements)

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“…However, Hut expression is not repressed by either glucose or ammonia (70). The identity of the hutH gene has been established (167). The hutH gene is unlinked to any other hut gene and is transcribed as a single-gene operon (168).…”

Section: Streptomyces Sppmentioning

confidence: 99%

Regulation of the Histidine Utilization (Hut) System in Bacteria

Bender

2012

Microbiol Mol Biol Rev

123

128

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SUMMARY The ability to degrade the amino acid histidine to ammonia, glutamate, and a one-carbon compound (formate or formamide) is a property that is widely distributed among bacteria. The four or five enzymatic steps of the pathway are highly conserved, and the chemistry of the reactions displays several unusual features, including the rearrangement of a portion of the histidase polypeptide chain to yield an unusual imidazole structure at the active site and the use of a tightly bound NAD molecule as an electrophile rather than a redox-active element in urocanase. Given the importance of this amino acid, it is not surprising that the degradation of histidine is tightly regulated. The study of that regulation led to three central paradigms in bacterial regulation: catabolite repression by glucose and other carbon sources, nitrogen regulation and two-component regulators in general, and autoregulation of bacterial regulators. This review focuses on three groups of organisms for which studies are most complete: the enteric bacteria, for which the regulation is best understood; the pseudomonads, for which the chemistry is best characterized; and Bacillus subtilis , for which the regulatory mechanisms are very different from those of the Gram-negative bacteria. The Hut pathway is fundamentally a catabolic pathway that allows cells to use histidine as a source of carbon, energy, and nitrogen, but other roles for the pathway are also considered briefly here.

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Section: Streptomyces Sppmentioning

confidence: 99%

Regulation of the Histidine Utilization (Hut) System in Bacteria

Bender

2012

Microbiol Mol Biol Rev

123

128

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“…The amino-terminal amino acid sequence of purified histidase indicates that translation of hutH initiates at the AUG beginning at position 835 (38). There was no evidence in our active histidase preparation of a protein that initiated transla- Because hutH is transcribed monocistronically in S. griseus, the organization of the hut genes is significantly different from that in other bacteria.…”

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confidence: 46%

“…The histidase structural gene from the wild-type strain of S. griseus has been cloned, and its nucleotide sequence has been determined (38). Here we describe our analysis of hutH expression, which demonstrates that, unlike the gene in other bacteria, hutH in S. griseus is transcribed as a monocistronic unit from a transcription start site that is coincident with the translation initiation site.…”

mentioning

confidence: 97%

“…The probe used in low-resolution nuclease protection studies (11) to map the approximate 5Ј end of the hutH transcript was generated by digesting pKK570 (an exonuclease III-derived deletion derivative of pKK540 [38]) with MluI and HindIII and labeling the 5Ј ends of the agarose gel-purified fragment (14) with polynucleotide kinase (33). To map the 3Ј end of the hutH transcript, the 3Ј ends formed by digestion of pKK548 (an exonuclease III-derived deletion derivative of pKK538 [38]) with MluI and HindIII were labeled by filling in the 3Ј ends with Klenow fragment and the appropriate deoxynucleotides (2). (The HindIII site in both cases was part of the polylinker cloning site, and the attached radiolabel was therefore hydrolyzed by subsequent exposure to S1 nuclease.)…”

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confidence: 99%

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Regulated expression of the histidase structural gene in Streptomyces griseus

Srinivasan

Kendrick

1995

J Bacteriol

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The histidase structural gene from Streptomyces griseus was expressed from a leaderless, monocistronic transcript. Multiple copies of the DNA located upstream of the hutH transcription initiation site led to a significant level of histidase activity when present in trans in the wild-type strain grown under noninducing conditions.In bacteria that utilize L-histidine as a carbon or nitrogen source, L-histidine is first deaminated by histidine ammonia lyase (histidase [20,24,26]), which is encoded by hutH. The ammonia released by histidase enters pathways for its assimilation. The other product of deamination, urocanate, is catabolized in several steps to form L-glutamate (20, 24). Urocanase, encoded by hutU, is required for the conversion of urocanate to imidazolonepropionate in this pathway (17,20,24).Examination of the regulated synthesis of histidase and urocanase by Bacillus subtilis, Klebsiella aerogenes, and Pseudomonas putida has led to the identification of one (28), two (6, 30), and three (9, 13) contiguous hut operons, respectively, that encode the enzymes required for conversion of L-histidine to L-glutamate. Although the order of hut genes differs among these species, hutH and hutU invariably lie within the same operon. Expression of these hut genes is regulated either by a repressor protein that binds at a site adjacent to the promoter and reduces initiation of transcription (12,34) or by a mechanism that appears to involve transcription antitermination (28). Expression of hut genes in these bacteria is also controlled by the global mechanisms of carbon catabolite repression (27,29,37) and nitrogen regulation (25,31) or by amino acid repression (1).Previous studies have demonstrated that L-histidine is a good nitrogen source for Streptomyces coelicolor (20) and Streptomyces griseus (22). In streptomycetes the enzymes of histidine catabolism are active whenever L-histidine or urocanate is present in the medium, regardless of the presence of other carbon or nitrogen sources (3,20,22). Thus, there is no evidence for carbon or nitrogen regulation of the histidine utilization (Hut) system in streptomycetes. On the basis of enzymological analyses, a Hut Ϫ mutant that we isolated appeared to constitutively synthesize inactive histidase that could be activated in vitro by exposure to an extract prepared from the wild-type strain (23). Earlier studies also indicated that histidase from S. griseus and S. coelicolor is a hysteretic enzyme that undergoes activation during the course of the reaction (19,22). In S. griseus, the hysteretic status of histidase appears to be dependent on the life cycle (22). Because this result suggested the possibility that the metabolic flux of L-histidine is regulated at least in part by the hysteretic activity of histidase, we wished to determine if histidase synthesis is also regulated in S. griseus.The histidase structural gene from the wild-type strain of S. griseus has been cloned, and its nucleotide sequence has been determined (38). Here we describe our analysis of hutH expr...

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“…Downstream of hutV, hutH2's gene product consists of a 478-aa hydrophilic protein with a predicted molecular mass of 49.7 kDa. This protein shows significant homology (38% identical residues) with human (56) and bacterial histidases (43,62), including a putative HutH already described in S. meliloti (accession number no. AF032903).…”

Section: Resultsmentioning

confidence: 99%

Characterization of a Sinorhizobium meliloti ATP-Binding Cassette Histidine Transporter Also Involved in Betaine and Proline Uptake

et al. 2000

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The symbiotic soil bacterium Sinorhizobium meliloti uses the compatible solutes glycine betaine and proline betaine for both protection against osmotic stress and, at low osmolarities, as an energy source. A PCR strategy based on conserved domains in components of the glycine betaine uptake systems from Escherichia coli (ProU) and Bacillus subtilis (OpuA and OpuC) allowed us to identify a highly homologous ATP-binding cassette (ABC) binding protein-dependent transporter in S. meliloti. This system was encoded by three genes (hutXWV) of an operon which also contained a fourth gene (hutH2) encoding a putative histidase, which is an enzyme involved in the first step of histidine catabolism. Site-directed mutagenesis of the gene encoding the periplasmic binding protein (hutX) and of the gene encoding the cytoplasmic ATPase (hutV) was done to study the substrate specificity of this transporter and its contribution in betaine uptake. These mutants showed a 50% reduction in high-affinity uptake of histidine, proline, and proline betaine and about a 30% reduction in low-affinity glycine betaine transport. When histidine was used as a nitrogen source, a 30% inhibition of growth was observed in hut mutants (hutX and hutH2). Expression analysis of the hut operon determined using a hutX-lacZ fusion revealed induction by histidine, but not by salt stress, suggesting this uptake system has a catabolic role rather than being involved in osmoprotection. To our knowledge, Hut is the first characterized histidine ABC transporter also involved in proline and betaine uptake.

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Purification of histidase from Streptomyces griseus and nucleotide sequence of the hutH structural gene

Cited by 26 publications

References 40 publications

Regulation of the Histidine Utilization (Hut) System in Bacteria

Regulation of the Histidine Utilization (Hut) System in Bacteria

Regulated expression of the histidase structural gene in Streptomyces griseus

Characterization of a Sinorhizobium meliloti ATP-Binding Cassette Histidine Transporter Also Involved in Betaine and Proline Uptake

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