Degradation of ornithine transcarbamylase in sporulating Bacillus subtilis cells

Neway, Justin O.; Switzer, Robert L.

doi:10.1128/jb.155.2.522-530.1983

Cited by 13 publications

(2 citation statements)

References 20 publications

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“…Under aerobic growth conditions or in early stationary phase, the OTCase of B. slibtilis becomes slightly inducible by arginine (243; Stalon, unpublished data). The physiological relevance of this phenomenon is not evident since B. sulbtilis does not possess a deiminase pathway (243) and since OTCase is not needed for arginine accumulation into spores (244). CPSase is also slightly inducible in stationary cells (263).…”

Section: Control Of Enzyme Synthesis In Other Procaryotesmentioning

confidence: 98%

See 1 more Smart Citation

Biosynthesis and metabolism of arginine in bacteria.

Cunin¹,

Glansdorff²,

Pierard³

et al. 1986

Microbiological Reviews

519

342

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Section: Control Of Enzyme Synthesis In Other Procaryotesmentioning

confidence: 98%

“…The physiological role of this induction by arginine is not known, but the enzyme synthesized under all conditions exhibits the same response towards antibodies against purified OTCase. This same enzyme is subject to inactivation followed by proteolytic degradation in sporulating cells (244).…”

Section: Enzymatic Steps and Regulation Of Metabolic Flowmentioning

confidence: 99%

Biosynthesis and metabolism of arginine in bacteria.

Cunin¹,

Glansdorff²,

Pierard³

et al. 1986

Microbiological Reviews

519

342

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A new alkaline serine protease from alkalophilic Bacillus sp.: Cloning, sequencing, and characterization of an intracellular protease

Yamagata

Ichishima

1995

Current Microbiology

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To obtain a new serine protease from alkalophilic Bacillus sp. NKS-21, shotgun cloning was carried out. As a result, a new protease gene was obtained. It encoded an intracellular serine protease (ISP-1) in which there was no signal sequence. The molecular weight was 34,624. The protease showed about 50% homology with those of intracellular serine proteases (ISP-1) from Bacillus subtilis, B. polymyxa, and alkalophilic Bacillus sp. No. 221. The amino acid residues that form the catalytic triad, Ser, His and Asp, were completely conserved in comparison with subtilisins (the extracellular proteases from Bacillus). The cloned intracellular protease was expressed in Escherichia coli, and its purification and characterization were carried out. The enzyme showed stability under alkaline condition at pH 10 and tolerance to surfactants. The cloned ISP-1 digested well nucleoproteins, clupein and salmin, for the substrates.

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Cloning and Sequencing of the Major Intracellular Serine Protease Gene of Bacillus Subtilis

Beppu¹,

Koide²,

Uozumi³

1986

Bacillus Molecular Genetics and Biotechnology Applications

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A Bacillus subtlis 2.7-kilobase DNA fragment containing an intracellular protease gene was cloned into Escherichia coli. The transformants produced an intracellular protease of approximately 35,000 Mr whose activity was inhibited by both phenylmethylsulfonyl fluoride and EDTA. Introduction of the fragment on a multicopy vector, pUBllO, into B. subtilis caused a marked increase in the level of the intracellular protease. The nucleotide sequence of the cloned fragment showed the presence of an open reading frame for a possible proenzyme of the major intracellular serine protease (ISP-I) of B. subtilis with an NH2-terminal 17-or 20-amino-acid extension. The total amino acid sequence of the protease deduced from the nucleotide sequence showed considerable homology with that of an extracellular serine protease, subtilisin. The transcriptional initiation site of the ISP-I gene was identified by nuclease Si mapping. No typical conserved sequence for promoters was found upstream of the open reading frame. An ISP-I-negative mutant of B. subtilis was constructed by integration of artificially deleted gene into the chromosome. The mutant sporulated normally in a nutritionally rich medium but showed decreased sporulation in a synthetic medium. The chloramphenicol resistance determinant of a plasmid integrated at the ISP-I locus was mapped by PBS1 transduction and was found to be closely linked to metC (99.5%).Bacillus subtilis produces a variety of extracellular and intracellular proteases. An alkaline serine protease (subtilisin), a neutral metalloprotease, and an esterase are secreted into media, whereas at least two intracellular serine proteases are produced within B. subtilis cells (7,22,24,34,35). The major intracellular serine protease here designated as ISP-I is characterized by its sensitivity to EDTA due to an absolute requirement for Ca2+ for stability and activity (35). The partial NH2-terminal amino acid sequence of ISP-I shows considerable homology with that of subtilisin (35). A minor serine protease (ISP-II), possessing trypsin-like substrate specificity, has also been found in B. subtilis cells (29,34).Essential roles have been postulated for these intracellular proteases during sporulation, possibly through the turnover of intracellular proteins (13, 33), the processing of spore coat protein precursors (15,16,29), and the inactivation of ornithine transcarbamylase and several other enzymes (17, 21). Involvement of ISP-I in sporulation was suggested from observations that a thermosensitive sporulation mutant of B. subtilis lost both its intracellular protease activity and sporulating ability at the restrictive temperature (10). Hageman and Carlton also isolated an ISP-I-deficient mutant which failed to sporulate normally (5). On the other hand, a mutant with temperature-sensitive ISP-II was shown to have several altered functions at the postexponential growth phase and to produce spores deficient in a major lowmolecular-weight coat polypeptide at the restrictive temperature (29).In this paper we describe th...

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Degradation of ornithine transcarbamylase in sporulating Bacillus subtilis cells

Cited by 13 publications

References 20 publications

Biosynthesis and metabolism of arginine in bacteria.

Biosynthesis and metabolism of arginine in bacteria.

A new alkaline serine protease from alkalophilic Bacillus sp.: Cloning, sequencing, and characterization of an intracellular protease

Cloning and Sequencing of the Major Intracellular Serine Protease Gene of Bacillus Subtilis

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