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. 1968 Feb;95(2):507–519. doi: 10.1128/jb.95.2.507-519.1968

Correlation Between Mutation Type and the Production of Cross-reacting Material in Mutants of the A Gene of the Histidine Operon in Salmonella typhimurium

Michael N Margolies a,1, Robert F Goldberger a
PMCID: PMC252047  PMID: 4966548

Abstract

This study concerns the correlation between the type of mutation in a bacterial gene and the ability of the mutant organism to produce immunologically cross-reacting material (CRM). Ninety-five mutants of the A gene of the histidine operon in Salmonella typhimurium have been separated into three classes, by means of mutagenesis and suppression tests, according to the classification scheme devised by H. J. Whitfield, Jr., et al.: (i) missense mutants (in which there is a single amino acid substitution in the A protein); (ii) nonsense mutants (in which various portions of the carboxyl-terminal segment of the A protein are missing); and (iii) deletion and frameshift mutants. Extracts of all mutants were also examined for the presence of CRM. At least 70% of the missense mutants produced CRM. The genetic loci affected in these mutants were randomly distributed throughout the A gene. None of the nonsense, deletion, or frameshift mutants produced CRM. The absence of CRM in the nonsense mutants is in keeping with the finding that removal of the carboxyl-terminal valine residue from the A protein by carboxypeptidase A eliminates antigenicity.

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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. AMES B. N., HARTMAN P. E., JACOB F. Chromosomal alterations affecting the regulation of histidine biosynthetic enzymes in Salmonella. J Mol Biol. 1963 Jul;7:23–42. doi: 10.1016/s0022-2836(63)80016-9. [DOI] [PubMed] [Google Scholar]
  3. AMES B. N., MARTIN R. G., GARRY B. J. The first step of histidine biosynthesis. J Biol Chem. 1961 Jul;236:2019–2026. [PubMed] [Google Scholar]
  4. Ames B. N., Garry B. COORDINATE REPRESSION OF THE SYNTHESIS OF FOUR HISTIDINE BIOSYNTHETIC ENZYMES BY HISTIDINE. Proc Natl Acad Sci U S A. 1959 Oct;45(10):1453–1461. doi: 10.1073/pnas.45.10.1453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ames B. N., Whitfield H. J., Jr Frameshift mutagenesis in Salmonella. Cold Spring Harb Symp Quant Biol. 1966;31:221–225. doi: 10.1101/sqb.1966.031.01.030. [DOI] [PubMed] [Google Scholar]
  6. Brenner S., Barnett L., Katz E. R., Crick F. H. UGA: a third nonsense triplet in the genetic code. Nature. 1967 Feb 4;213(5075):449–450. doi: 10.1038/213449a0. [DOI] [PubMed] [Google Scholar]
  7. Brenner S., Stretton A. O., Kaplan S. Genetic code: the 'nonsense' triplets for chain termination and their suppression. Nature. 1965 Jun 5;206(988):994–998. doi: 10.1038/206994a0. [DOI] [PubMed] [Google Scholar]
  8. CRICK F. H., BARNETT L., BRENNER S., WATTS-TOBIN R. J. General nature of the genetic code for proteins. Nature. 1961 Dec 30;192:1227–1232. doi: 10.1038/1921227a0. [DOI] [PubMed] [Google Scholar]
  9. KIRCHNER C. E. The effects of the mutator gene on molecular changes and mutation of Salmonella typhimurium. J Mol Biol. 1960 Dec;2:331–338. doi: 10.1016/s0022-2836(60)80044-7. [DOI] [PubMed] [Google Scholar]
  10. LOPER J. C., ADAMS E. PURIFICATION AND PROPERTIES OF HISTIDINOL DEHYDROGENASE FROM SALMONELLA TYPHIMURIUM. J Biol Chem. 1965 Feb;240:788–795. [PubMed] [Google Scholar]
  11. LOPER J. C., GRABNAR M., STAHL R. C., HARTMAN Z., HARTMAN P. E. GENES AND PROTEINS INVOLVED IN HISTIDINE BIOSYNTHESIS IN SALMONELLA. Brookhaven Symp Biol. 1964 Dec;17:15–52. [PubMed] [Google Scholar]
  12. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  13. Margolies M. N., Goldberger R. F. Isolation of the fourth (isomerase) of histidine biosynthesis from Salmonella typhimurium. J Biol Chem. 1966 Jul 25;241(14):3262–3269. [PubMed] [Google Scholar]
  14. Margolies M. N., Goldberger R. F. Physical and chemical characterization of the isomerase of histidine biosynthesis in Salmonella typhimurium. J Biol Chem. 1967 Jan 25;242(2):256–264. [PubMed] [Google Scholar]
  15. Martin R. G., Goldberger R. F. Imidazolylacetolphosphate:L-glutamate aminotransferase. Purification and physical properties. J Biol Chem. 1967 Mar 25;242(6):1168–1174. [PubMed] [Google Scholar]
  16. Martin R. G., Silbert D. F., Smith W. E., Whitfield H. J., Jr Polarity in the histidine operon. J Mol Biol. 1966 Nov 14;21(2):357–369. doi: 10.1016/0022-2836(66)90104-5. [DOI] [PubMed] [Google Scholar]
  17. Miyake T. Mutator Factor in Salmonella Typhimurium. Genetics. 1960 Jan;45(1):11–14. doi: 10.1093/genetics/45.1.11. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Newton W. A., Beckwith J. R., Zipser D., Brenner S. Nonsense mutants and polarity in the lac operon of Escherichia coli. J Mol Biol. 1965 Nov;14(1):290–296. doi: 10.1016/s0022-2836(65)80250-9. [DOI] [PubMed] [Google Scholar]
  19. PREER J. R., Jr A quantitative study of a technique of double diffusion in agar. J Immunol. 1956 Jul;77(1):52–60. [PubMed] [Google Scholar]
  20. Roth J. R., Antón D. N., Hartman P. E. Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties. J Mol Biol. 1966 Dec 28;22(2):305–323. doi: 10.1016/0022-2836(66)90134-3. [DOI] [PubMed] [Google Scholar]
  21. SARABHAI A. S., STRETTON A. O., BRENNER S., BOLLE A. CO-LINEARITY OF THE GENE WITH THE POLYPEPTIDE CHAIN. Nature. 1964 Jan 4;201:13–17. doi: 10.1038/201013a0. [DOI] [PubMed] [Google Scholar]
  22. SMITH D. W., AMES B. N. INTERMEDIATES IN THE EARLY STEPS OF HISTIDINE BIOSYNTHESIS. J Biol Chem. 1964 Jun;239:1848–1855. [PubMed] [Google Scholar]
  23. SUSKIND S. R., WICKHAM M. L., CARSIOTIS M. Antienzymes in immunogenetic studies. Ann N Y Acad Sci. 1963 May 8;103:1106–1127. doi: 10.1111/j.1749-6632.1963.tb53762.x. [DOI] [PubMed] [Google Scholar]
  24. 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]
  25. 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]
  26. Weigert M. G., Garen A. Base composition of nonsense codons in E. coli. Evidence from amino-acid substitutions at a tryptophan site in alkaline phosphatase. Nature. 1965 Jun 5;206(988):992–994. doi: 10.1038/206992a0. [DOI] [PubMed] [Google Scholar]
  27. Whitfield H. J., Jr, Martin R. G., Ames B. N. Classification of aminotransferase (C gene) mutants in the histidine operon. J Mol Biol. 1966 Nov 14;21(2):335–355. doi: 10.1016/0022-2836(66)90103-3. [DOI] [PubMed] [Google Scholar]

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