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Gene Review

hisD  -  histidinol dehydrogenase

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

 
 
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Disease relevance of hisD

  • We have studied a very unusual strong polar mutant in the intercistronic barrier between the second (hisD) and third (hisC) cistrons of the histidine operon of Salmonella typhimurium to obtain further insights into the molecular mechanisms leading to transcription termination within cistrons [1].
 

High impact information on hisD

 

Chemical compound and disease context of hisD

  • The biochemistry of interallelic complementation within the Salmonella typhimurium hisD gene was investigated by in vitro protein complementation of mutant histidinol dehydrogenases (EC 1.1.1.23) [5].
  • From the results of the studies on Salmonella typhimurium HDH, it has been proposed that one of these two conserved Cys residues is involved in the thiohemiacetal formation at the aldehyde oxidation step [Grubmeyer and Gray (1986) Biochemistry 25, 4778-4784] [6].
 

Biological context of hisD

  • A total of 12 Salmonella typhimurium mutants were selected with mutations in the minor tRNAProGGG which suppress a +1 frameshift mutation in the hisD gene [7].
  • Chromosome rearrangements that juxtapose the hisD gene and a foreign promoter are obtained by this selection [8].
  • The presence of transposons Tn10 or Tn5 in the genome increases the frequency with which a silent (promoter-less) gene (hisD) is mutationally activated [9].
  • DNA fragments containing the promoter/regulatory region and the first two structural genes of the histidine operon (hisOGD) were identified by their ability to direct regulated synthesis of histidinol dehydrogenase (product of hisD) in a coupled in vitro protein synthesizing system [10].
  • Directed translocation of an expressed gene (hisD) provided strains to test for position effects on gene expression in Salmonella typhimurium [11].
 

Associations of hisD with chemical compounds

 

Other interactions of hisD

  • Transduction studies demonstrated that mutations of his+ were closely linked to the hisD gene, and probably were in the structural hisG gene itself [16].
  • One of the two B.rfb+ gene clusters of a (P22-lysogenic) S. typhimurium strain with a tandem duplication of a chromosomal segment including hisD and B.rfb+ was replaced (by transduction) by a D.rfb+ gene cluster; the resulting strain was O1+ O4+ O5+ O9+ and stable as such after being made recA [17].
 

Analytical, diagnostic and therapeutic context of hisD

  • The hisD selection is being tested for potential use in gene targeting experiments with mouse embryonic stem (ES) cells [3].
  • To clarify the reaction mechanism, we investigated the role of the conserved Cys residues by site-directed mutagenesis in cabbage HDH [6].

References

  1. In vivo analysis of the mechanisms responsible for strong transcriptional polarity in a "sense" mutant within an intercistronic region. Alifano, P., Ciampi, M.S., Nappo, A.G., Bruni, C.B., Carlomagno, M.S. Cell (1988) [Pubmed]
  2. Amino acid sequence of ATP phosphoribosyltransferase of Salmonella typhimurium. Piszkiewicz, D., Tilley, B.E., Rand-Meir, T., Parsons, S.M. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  3. Transgenic mice for the establishment of histidinol-resistant embryonic fibroblast feeder layers. Tucker, R.M., Burke, D.T. FASEB J. (1996) [Pubmed]
  4. Conserved cysteine residues of histidinol dehydrogenase are not involved in catalysis. Novel chemistry required for enzymatic aldehyde oxidation. Teng, H., Segura, E., Grubmeyer, C. J. Biol. Chem. (1993) [Pubmed]
  5. Purification and in vitro complementation of mutant histidinol dehydrogenases. Lee, S.Y., Grubmeyer, C.T. J. Bacteriol. (1987) [Pubmed]
  6. Site-directed mutagenesis shows that the conserved cysteine residues of histidinol dehydrogenase are not essential for catalysis. Nagai, A., Kheirolomoom, A., Ohta, D. J. Biochem. (1993) [Pubmed]
  7. Structural alterations far from the anticodon of the tRNAProGGG of Salmonella typhimurium induce +1 frameshifting at the peptidyl-site. Qian, Q., Björk, G.R. J. Mol. Biol. (1997) [Pubmed]
  8. Selection and endpoint distribution of bacterial inversion mutations. Schmid, M.B., Roth, J.R. Genetics (1983) [Pubmed]
  9. Activation of silent genes by transposons Tn5 and Tn10. Wang, A., Roth, J.R. Genetics (1988) [Pubmed]
  10. Use of M13mp phages to study gene regulation, structure and function: cloning and recombinational analysis of genes of the Salmonella typhimurium histidine operon. Artz, S., Holzschu, D., Blum, P., Shand, R. Gene (1983) [Pubmed]
  11. Gene location affects expression level in Salmonella typhimurium. Schmid, M.B., Roth, J.R. J. Bacteriol. (1987) [Pubmed]
  12. Deletions fusing the hisG and hisD genes in Salmonella typhimurium. Ino, I., Hartman, P.E., Hartman, Z., Yourno, J. J. Bacteriol. (1975) [Pubmed]
  13. Mutagenesis of histidinol dehydrogenase reveals roles for conserved histidine residues. Teng, H., Grubmeyer, C. Biochemistry (1999) [Pubmed]
  14. A cysteine residue (cysteine-116) in the histidinol binding site of histidinol dehydrogenase. Grubmeyer, C.T., Gray, W.R. Biochemistry (1986) [Pubmed]
  15. L-histidinol dehydrogenase, a Zn2+-metalloenzyme. Grubmeyer, C., Skiadopoulos, M., Senior, A.E. Arch. Biochem. Biophys. (1989) [Pubmed]
  16. The mutagenicity of sodium bisulfite on base-substitution strains of Salmonella typhimurium. De Giovanni-Donnelly, R. Teratog., Carcinog. Mutagen. (1985) [Pubmed]
  17. Construction of Salmonella strains with both antigen O4 (of group B) and antigen O9 (of group D). Johnson, B.N., Weintraub, A., Lindberg, A.A., Stocker, B.A. J. Bacteriol. (1992) [Pubmed]
 
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