Evolutionary Mechanism of Adaptation of Arthrobacter histidinolovorans and Pseudomonas aeruginosa to Use L-Histidinol as a Sole Source of Nitrogen and Carbon

Dhawale, Motiram R.; Creaser, E. H.; Loper, John C.

doi:10.1099/00221287-73-2-353

Cited by 10 publications

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“…1 .23), which is coded by the structural gene hisD, catalyses the last step in the biosynthesis of histidine, namely the oxidation of histidinol to histidine with the concomitant reduction of 2 mol of NAD+ per rnol of histidine formed (Loper, 1968). Histidinol dehydrogenase (HDH) has been partially purified from Arthrobacter histidinolovorans (Dhawale et al, 1972), Neurospora crassa (Minson & Creaser, 1969), yeast (Keesey et al, 1979), Bacillus spp. (Lindsay & Creaser, 1977), Salmonella typhimuriurn (Yourno & Ino, 1968;Loper, 1968) and Escherichia coli K12 (Bitar et al, 1977).…”

Section: Introductionmentioning

confidence: 99%

Purification and Properties of Histidinol Dehydrogenase from Escherichia coli B

Andorn

Aronovitch

1982

Microbiology

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Histidinol dehydrogenase has been purified from a derepressed mutant of Escherichia coli B. A molecular weight of about 91,000 was estimated by gel filtration. The native enzyme seems to be composed of two similar subunits which have a molecular weight of 52,000 as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The pI of the enzyme as determined by isoelectric focusing is 4.75. The enzyme is maximally active at pH 9.5. It is highly specific for NAD+ and histidinol, with a Km (NAD+) of 0.57 mM and a Km (histidinol) of 14 microM. Mn2+ is required for maximal activity. The enzyme is completely inactivated by 8 M-urea but regains its activity very quickly upon removal of the urea. Mn2+ and histidinol protect the enzyme from heat inactivation.

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Section: Introductionmentioning

confidence: 99%

Purification and Properties of Histidinol Dehydrogenase from Escherichia coli B

Andorn

Aronovitch

1982

Microbiology

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“…(Minson & Creaser, 1969). In Arthrobacter histidinolovorans, which can use histidinol as a sole source of carbon and nitrogen (Adams, 1954), two enzymes can be produced, both specific for the dehydrogenation of histidinol; one is the normal biosynthetic enzyme, the second is only produced when histidinol is present in the medium (Dhawale et al, 1972).…”

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Purification and properties of histidinol dehydrogenases from psychrophilic, mesophilic and thermophilic bacilli

Lindsay¹,

Creaser²

1977

Biochemical Journal

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As a first step in elucidating one molecular mechanism of adaptation to life at extreme temperatures, we purified and characterized the enzyme histidinol dehydrogenase (EC 1.1.1.23) from a number of bacilli whose growth temperatures range from 5 degrees t to 90 degrees C. The enzymes were purified by (NH4)2SO4 precipitation, ion-exchange chromatography on Sephadex, affinity chromatography on histamine- or histidine-Sepharose and preparative gradient gel electrophoresis. All had similar mol.wts. (29200), sedimentation coefficients (S20,w 2.56S), affinities for histidinol and NAD+ (Km = 48 micron and 0.2 mM respectively) and all had pH optima at 9.6. Marked differences were observed in stability with respect to temperature and the temperature at which the initial velocity for histidinol dehydrogenation was optimal. These optima range from 25 degrees C for the enzyme from the psychrophilic species through to 41 degrees C for the mesophiles to 85-92 degrees C for the extreme thermophiles. It is concluded that the ability of the enzymes to operate at their various optimum temperatures is an intrinsic property of their amino acid sequences.

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“…This mutant can utilize L-histidinol as sole source of carbon and nitrogen and has a 60-fold increased histidinol dehydrogenase (HDH) content (Dhawale, Creaser & Loper, 1972). Transductional analysis was carried out using I 8 histidine-requiring mutants to see where the hnc-I locus maps in relation to the structural genes of histidine biosynthesis.…”

Section: S U M M a R Ymentioning

confidence: 99%

Analysis of an L-Histidinol-utilizing Mutant of Pseudomonas aeruginosa

Dhawale

Creaser

1975

Journal of General Microbiology

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S U M M A R YTransductional analysis was applied to the Pseudomonas aeruginosa mutant P A O I~ (hnc-I). This mutant can utilize L-histidinol as sole source of carbon and nitrogen and has a 60-fold increased histidinol dehydrogenase (HDH) content (Dhawale, Creaser & Loper, 1972). Transductional analysis was carried out using I 8 histidine-requiring mutants to see where the hnc-I locus maps in relation to the structural genes of histidine biosynthesis. The hnc-I marker cotransduced with group IV genes at 97 to IOO % and not at all with group I, which is known to be the structural gene for HDH.The data obtained in the studies of K , (histidinol) and K, (NAD), and the effect of pH and temperature on the HDH activity from PAOI and P A O I~ are in full agreement with the genetic data that the hnc-I mutation is not in the structural gene for HDH. It is suggested that hnc-I may be a mutation in a regulatory gene affecting HDH synthesis in P A O I~ and may map close to his-ZV whose function in histidine biosynthesis is not known. I N T R O D U C T I O NPrevious work on the evolution of mechanisms for utilization of histidinol as sole source of carbon and nitrogen (Dhawale, Creaser & Loper, 1 9 7 2 ) showed that whereas Arthrobacter histidinolovorans produced a second, inducible enzyme system for the conversion of histidinol to histidine, Pseudomonas aeruginosa appeared to have developed a new control system for the increased formation of histidinol dehydrogenase (HDH).We isolated a mutant of P . aeruginosa which can utilize histidinol (hnc-I: P A O I~) as the sole source of nitrogen and carbon, and gives a 60-fold increase in total HDH activity. However, polyacrylamide gel electrophoresis was unable to separate the enzyme activity of the mutant from that obtained from the parent strain PAOI grown on glucose plus minimal medium. The 'mutant' enzyme is inducible by histidinol and its synthesis is repressed by the catabolites of histidinol and histidine. It has been suggested that HDH produced by the mutant strain P A O I~ is the same as that synthesized by the wild-type strain (PAOI) grown on mineral salts, glucose and NH,NO,. To test this hypothesis further, two approaches were used. Firstly, a genetic analysis was carried out using histidine-requiring mutants in order to relate the hnc-I mutation to other genes of histidine biosynthesis in this bacterium. Secondly, the kinetic properties of the enzymes, which included K , (histidinol), K , (NAD), optimum pH and optimum temperature of the enzyme reaction were studied.There appear to be at least five groups of genes involved in histidine biosynthesis in P.

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Evolutionary Mechanism of Adaptation of Arthrobacter histidinolovorans and Pseudomonas aeruginosa to Use L-Histidinol as a Sole Source of Nitrogen and Carbon

Cited by 10 publications

References 0 publications

Purification and Properties of Histidinol Dehydrogenase from Escherichia coli B

Purification and Properties of Histidinol Dehydrogenase from Escherichia coli B

Purification and properties of histidinol dehydrogenases from psychrophilic, mesophilic and thermophilic bacilli

Analysis of an L-Histidinol-utilizing Mutant of Pseudomonas aeruginosa

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