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. 1975 Sep;123(3):1254–1264. doi: 10.1128/jb.123.3.1254-1264.1975

Deletions fusing the hisG and hisD genes in Salmonella typhimurium.

I Ino, P E Hartman, Z Hartman, J Yourno
PMCID: PMC235849  PMID: 1099075

Abstract

Frameshift mutation hisD497 occurs in the operator-proximal portion of the Salmonella typhimurium gene coding for the dimeric protein, L-histidinol dehydrogenase (HDH). Rare revertants of hisD497 are deletions fusing the hisD gene to the adjacent preceding structural gene, hisG (adenosine 5'-triphosphate-PR transferase). HDH purified from one revertant, hisGD4908, contains subunits of approximately normal molecular weight but with no clearly demonstrable unique amino-terminal sequence. We propose that a combined inactive G-D polypeptide is synthesized and then cleaved at a number of closely juxtaposed sites by endoproteolytic activity. At least some of the resulting fragments then participate in formation of active HDH dimers.

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Selected References

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  1. AMES B. N., GARRY B., HERZENBERG L. A. The genetic control of the enzymes of histidine biosynthesis in Salmonella typhimurium. J Gen Microbiol. 1960 Apr;22:369–378. doi: 10.1099/00221287-22-2-369. [DOI] [PubMed] [Google Scholar]
  2. Case M. E., Giles N. H. Revertants and secondary arom-2 mutants induced in non-complementing mutants in the arom gene cluster of Neurospora crassa. Genetics. 1974 Aug;77(4):613–626. doi: 10.1093/genetics/77.4.613. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Edman P., Begg G. A protein sequenator. Eur J Biochem. 1967 Mar;1(1):80–91. doi: 10.1007/978-3-662-25813-2_14. [DOI] [PubMed] [Google Scholar]
  4. Fink G. R., Klopotowski T., Ames B. N. Histidine regulatory mutants in Salmonella typhimurium. IV. A positive selection for polar histidine-requiring mutants from histidine operator constitutive mutants. J Mol Biol. 1967 Nov 28;30(1):81–95. doi: 10.1016/0022-2836(67)90245-8. [DOI] [PubMed] [Google Scholar]
  5. Goldberger R. F. Autogenous regulation of gene expression. Science. 1974 Mar 1;183(4127):810–816. doi: 10.1126/science.183.4127.810. [DOI] [PubMed] [Google Scholar]
  6. Greeb J., Atkins J. F., Loper J. C. Histidinol dehydrogenase (his D) mutants of Salmonella typhimurium. J Bacteriol. 1971 May;106(2):421–431. doi: 10.1128/jb.106.2.421-431.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hartman P. E., Hartman Z., Stahl R. C. Classification and mapping of spontaneous and induced mutations in the histidine operon of Salmonella. Adv Genet. 1971;16:1–34. doi: 10.1016/s0065-2660(08)60352-1. [DOI] [PubMed] [Google Scholar]
  8. Hartman P. E. Some improved methods in P22 transduction. Genetics. 1974 Apr;76(4):625–631. doi: 10.1093/genetics/76.4.625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Holland J. J., Kiehn E. D. Specific cleavage of viral proteins as steps in the synthesis and maturation of enteroviruses. Proc Natl Acad Sci U S A. 1968 Jul;60(3):1015–1022. doi: 10.1073/pnas.60.3.1015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Houston L. L. Evidence for proteolytic degradation of histidinol phosphate phosphatase specified by nonsense mutants of the hisB gene of Salmonella typhimurium. J Bacteriol. 1973 Oct;116(1):88–97. doi: 10.1128/jb.116.1.88-97.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Ino I., Yourno J. X-ray mutagenesis: base-pair deletion at a frameshift hotspot in Salmonella. J Mol Biol. 1974 May 15;85(2):301–307. doi: 10.1016/0022-2836(74)90365-9. [DOI] [PubMed] [Google Scholar]
  12. Isono K., Yourno J. Mutation leading to gene fusion in the histidine operon of Salmonella typhimurium. J Mol Biol. 1973 Jun 5;76(4):455–461. doi: 10.1016/0022-2836(73)90484-1. [DOI] [PubMed] [Google Scholar]
  13. Isono S., Yourno J. Non-suppressible addition frameshift in Salmonella. J Mol Biol. 1974 Jan 25;82(3):355–360. doi: 10.1016/0022-2836(74)90596-8. [DOI] [PubMed] [Google Scholar]
  14. Jacobson M. F., Baltimore D. Polypeptide cleavages in the formation of poliovirus proteins. Proc Natl Acad Sci U S A. 1968 Sep;61(1):77–84. doi: 10.1073/pnas.61.1.77. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kono T., Yourno J. Proteolytic release of a histidinol dehydrogenase fragment from the double enzyme histidinol dehydrogenase-imidazolylacetol-phosphate: L-glutamate aminotransferase. J Biol Chem. 1971 Apr 10;246(7):2203–2206. [PubMed] [Google Scholar]
  16. Loper J. C. Histidinol dehydrogenase from Salmonella typhimurium. Crystallization and composition studies. J Biol Chem. 1968 Jun 25;243(12):3264–3272. [PubMed] [Google Scholar]
  17. Murray M. L., Hartman P. E. Overproduction of hisH and hisF gene products leads to inhibition of cell cell division in Salmonella. Can J Microbiol. 1972 May;18(5):671–681. doi: 10.1139/m72-105. [DOI] [PubMed] [Google Scholar]
  18. Parsons S. M., Koshland D. E., Jr Multiple aggregation states of phosphoribosyladenosine triphosphate synthetase. J Biol Chem. 1974 Jul 10;249(13):4119–4126. [PubMed] [Google Scholar]
  19. Pine M. J. Turnover of intracellular proteins. Annu Rev Microbiol. 1972;26:103–126. doi: 10.1146/annurev.mi.26.100172.000535. [DOI] [PubMed] [Google Scholar]
  20. Pisano J. J., Bronzert T. J. Analysis of amino acid phenylthiohydantoins by gas chromatography. J Biol Chem. 1969 Oct 25;244(20):5597–5607. [PubMed] [Google Scholar]
  21. Prouty W. F., Goldberg A. L. Effects of protease inhibitors on protein breakdown in Escherichia coli. J Biol Chem. 1972 May 25;247(10):3341–3352. [PubMed] [Google Scholar]
  22. Tanemura S., Yourno J. Frameshift revertant of Salmonella typhimurium producing histidinol dehydrogenase with a sequence of four extra amino acid residues. J Mol Biol. 1969 Dec 28;46(3):459–466. doi: 10.1016/0022-2836(69)90189-2. [DOI] [PubMed] [Google Scholar]
  23. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  24. Voll M. J., Appella E., Martin R. G. Purification and composition studies of phosphoribosyladenosine triphosphate:pyrophosphate phosphoribosyltransferase, the first enzyme of histidine biosynthesis. J Biol Chem. 1967 Apr 25;242(8):1760–1767. [PubMed] [Google Scholar]
  25. Voll M. J. Derivation of an F-merogenote and a phi-80 high-frequency transducing phage carrying the histidine operon os Salmonella. J Bacteriol. 1972 Feb;109(2):741–750. doi: 10.1128/jb.109.2.741-750.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Voll M. J., Shiller L. M., Castrilli J. His-linked hydrogen sulfide locus in Salmonella typhimurium. J Bacteriol. 1974 Nov;120(2):902–905. doi: 10.1128/jb.120.2.902-905.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Voll M. J. Translation and polarity in the histidine operon. 3. The isolation of prototrophic polar mutations. J Mol Biol. 1967 Nov 28;30(1):109–124. doi: 10.1016/0022-2836(67)90247-1. [DOI] [PubMed] [Google Scholar]
  28. Whitfield H. J., Jr, Gutnick D. L., Margolies M. N., Martin R. G., Rechler M. M., Voll M. J. Relative translation frequencies of the cistrons of the histidine operon. J Mol Biol. 1970 Apr 14;49(1):245–249. doi: 10.1016/0022-2836(70)90391-8. [DOI] [PubMed] [Google Scholar]
  29. Yourno J. Composition and subunit structure of histidinol dehydrogenase from Salmonella typhimurium. J Biol Chem. 1968 Jun 25;243(12):3277–3288. [PubMed] [Google Scholar]
  30. Yourno J., Heath S. Nature of the hisD3018 frameshift mutation in Salmonella typhimurium. J Bacteriol. 1969 Oct;100(1):460–468. doi: 10.1128/jb.100.1.460-468.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Yourno J., Ino I. Purification and crystallization of histidinol dehydrogenase from Salmonella typhimurium LT-2. J Biol Chem. 1968 Jun 25;243(12):3273–3276. [PubMed] [Google Scholar]
  32. Yourno J. Nature of the compensating frameshift in the double frameshift mutant hisD3018 R5 of Salmonella typhimurium. J Mol Biol. 1970 Mar;48(3):437–442. doi: 10.1016/0022-2836(70)90056-2. [DOI] [PubMed] [Google Scholar]
  33. Yourno J. Similarity of cross-suppressible frameshifts in Salmonella typhimurium. J Mol Biol. 1971 Nov 28;62(1):223–231. doi: 10.1016/0022-2836(71)90141-0. [DOI] [PubMed] [Google Scholar]

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