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. 1972 Jun;110(3):793–802. doi: 10.1128/jb.110.3.793-802.1972

Enzyme Evolution in the Enterobacteriaceae1

Gary T Cocks a,2, Allan C Wilson a
PMCID: PMC247495  PMID: 4113124

Abstract

An immunological approach has been used for the study of alkaline phosphatase evolution in bacteria of the family Enterobacteriaceae. Antisera were prepared against alkaline phosphatase from Escherichia coli and Klebsiella aerogenes and tested against the unpurified alkaline phosphatases of 32 strains of enterobacteria by double diffusion and quantitative micro-complement fixation. The immunological relationships detected among the alkaline phosphatases of enterobacteria agree approximately with those reported for five other enzymes, as well as with the tryptic peptide pattern similarities found for two other enzymes, and with the relationships detected by interspecific deoxyribonucleic acid hybridization tests.

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Selected References

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  1. Air G. M., Thompson E. O., Richardson B. J., Sharman G. B. Amino-acid sequences of kangaroo myoglobin and haemoglobin and the date of marsupial-eutherian divergence. Nature. 1971 Feb 5;229(5284):391–394. doi: 10.1038/229391a0. [DOI] [PubMed] [Google Scholar]
  2. Arnheim N., Jr, Cocks G. T., Wilson A. C. Molecular size of hagfish muscle lactate dehydrogenase. Science. 1967 Aug 4;157(3788):568–569. doi: 10.1126/science.157.3788.568. [DOI] [PubMed] [Google Scholar]
  3. Arnheim N., Prager E. M., Wilson A. C. Immunological prediction of sequence differences among proteins. Chemical comparison of chicken, quail, and phesant lysozymes. J Biol Chem. 1969 Apr 25;244(8):2085–2094. [PubMed] [Google Scholar]
  4. Baptist J. N., Shaw C. R., Mandel M. Zone electrophoresis of enzymes in bacterial taxonomy. J Bacteriol. 1969 Jul;99(1):180–188. doi: 10.1128/jb.99.1.180-188.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bascomb S., Lapage S. P., Willcox W. R., Curtis M. A. Numerical classification of the tribe Klebsielleae. J Gen Microbiol. 1971 Jun;66(3):279–295. doi: 10.1099/00221287-66-3-279. [DOI] [PubMed] [Google Scholar]
  6. Bowman J. E., Brubaker R. R., Frischer H., Carson P. E. Characterization of enterobacteria by starch-gel electrophoresis of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase. J Bacteriol. 1967 Sep;94(3):544–551. doi: 10.1128/jb.94.3.544-551.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Brenner D. J., Fanning G. R., Johnson K. E., Citarella R. V., Falkow S. Polynucleotide sequence relationships among members of Enterobacteriaceae. J Bacteriol. 1969 May;98(2):637–650. doi: 10.1128/jb.98.2.637-650.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. COHN M., TORRIANI A. M. The relationships in biosynthesis of the beta-galactosidase- and Pz-proteins in Escherichia coli. Biochim Biophys Acta. 1953 Feb;10(2):280–289. doi: 10.1016/0006-3002(53)90251-0. [DOI] [PubMed] [Google Scholar]
  9. Cocks G. T., Wilson A. C. Immunological detection of single amino acid substitutions in alkaline phosphatase. Science. 1969 Apr 11;164(3876):188–189. doi: 10.1126/science.164.3876.188. [DOI] [PubMed] [Google Scholar]
  10. Creighton T. E., Helinski D. R., Somerville R. L., Yanofsky C. Comparison of the tryptophan synthetase alpha-subunits of several species of Enterobacteriaceae. J Bacteriol. 1966 May;91(5):1819–1826. doi: 10.1128/jb.91.5.1819-1826.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Dickerson R. E. The structures of cytochrome c and the rates of molecular evolution. J Mol Evol. 1971;1(1):26–45. doi: 10.1007/BF01659392. [DOI] [PubMed] [Google Scholar]
  12. Durand A. M., Blazevic D. J. Differentiation of Serratia from Enterobacter on the basis of nucleoside phosphotransferase production. Appl Microbiol. 1970 Jan;19(1):134–137. doi: 10.1128/am.19.1.134-137.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Dvorak H. F., Brockman R. W., Heppel L. A. Purification and properties of two acid phosphatase fractions isolated from osmotic shock fluid of Escherichia coli. Biochemistry. 1967 Jun;6(6):1743–1751. doi: 10.1021/bi00858a024. [DOI] [PubMed] [Google Scholar]
  14. Fitch W. M., Margoliash E. Construction of phylogenetic trees. Science. 1967 Jan 20;155(3760):279–284. doi: 10.1126/science.155.3760.279. [DOI] [PubMed] [Google Scholar]
  15. GOMORI G. Alkaline phosphatase of cell nuclei. J Lab Clin Med. 1951 Apr;37(4):526–531. [PubMed] [Google Scholar]
  16. Gasser F., Gasser C. Immunological relationships among lactic dehydrogenases in the genera Lactobacillus and Leuconostoc. J Bacteriol. 1971 Apr;106(1):113–125. doi: 10.1128/jb.106.1.113-125.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Gordon J., Schweiger M., Krisko I., Williams C. A. Specificity and evolutionary divergence of the antigenic structure of the polypeptide chain elongation factors. J Bacteriol. 1969 Oct;100(1):1–4. doi: 10.1128/jb.100.1.1-4.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. King J. L., Jukes T. H. Non-Darwinian evolution. Science. 1969 May 16;164(3881):788–798. doi: 10.1126/science.164.3881.788. [DOI] [PubMed] [Google Scholar]
  19. Krieg R. E., Lockhart W. R. Classification of enterobacteria based on overall similarity. J Bacteriol. 1966 Nov;92(5):1275–1280. doi: 10.1128/jb.92.5.1275-1280.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. MCCARTHY B. J., BOLTON E. T. An approach to the measurement of genetic relatedness among organisms. Proc Natl Acad Sci U S A. 1963 Jul;50:156–164. doi: 10.1073/pnas.50.1.156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Mandel M. New approaches to bacterial taxonomy: perspective and prospects. Annu Rev Microbiol. 1969;23:239–274. doi: 10.1146/annurev.mi.23.100169.001323. [DOI] [PubMed] [Google Scholar]
  22. Margoliash E., Nisonoff A., Reichlin M. Immunological activity of cytochrome c. I. Precipitating antibodies to monomeric vertebrate cytochromes c. J Biol Chem. 1970 Mar 10;245(5):931–939. [PubMed] [Google Scholar]
  23. McQuade J. F., 3rd, Creighton T. E. Purification and comparison of the N-(5'-phosphoribosyl)anthranilic acid isomerase-indole-3-glycerol phosphate synthetase of tryptophan biosynthesis from three species of Enterobacteriaceae. Eur J Biochem. 1970 Oct;16(2):199–207. doi: 10.1111/j.1432-1033.1970.tb01072.x. [DOI] [PubMed] [Google Scholar]
  24. Murphy T. M., Mills S. E. Immunochemical and enzymatic comparisons of the tryptophan synthase alpha subunits from five species of Enterobacteriaceae. J Bacteriol. 1969 Mar;97(3):1310–1320. doi: 10.1128/jb.97.3.1310-1320.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Ota T., Kimura M. On the constancy of the evolutionary rate of cistrons. J Mol Evol. 1971;1(1):18–25. doi: 10.1007/BF01659391. [DOI] [PubMed] [Google Scholar]
  26. POULIK M. D. Starch gel electrophoresis in a discontinous system of buffers. Nature. 1957 Dec 28;180(4600):1477–1479. doi: 10.1038/1801477a0. [DOI] [PubMed] [Google Scholar]
  27. Prager E. M., Wilson A. C. The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. I. Micro-complement fixation studies. J Biol Chem. 1971 Oct 10;246(19):5978–5989. [PubMed] [Google Scholar]
  28. Prager E. M., Wilson A. C. The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. II. Comparison of precipitin and micro-complement fixation results. J Biol Chem. 1971 Nov 25;246(22):7010–7017. [PubMed] [Google Scholar]
  29. Rohlfing S. R., Crawford I. P. Partial purification and physical properties of Bacillus megaterium beta-galactosidase. J Bacteriol. 1966 Oct;92(4):1258–1259. doi: 10.1128/jb.92.4.1258-1259.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Rohlfing S. R., Crawford I. P. Purification and characterization of the beta-galactosidase of Aeromonas formicans. J Bacteriol. 1966 Mar;91(3):1085–1097. doi: 10.1128/jb.91.3.1085-1097.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. SIGNER E. R., TORRIANI A., LEVINTHAL C. Gene expression in intergeneric merozygotes. Cold Spring Harb Symp Quant Biol. 1961;26:31–34. doi: 10.1101/sqb.1961.026.01.008. [DOI] [PubMed] [Google Scholar]
  32. Sarich V. M. Pinniped origins and the rate of evolution of carnivore albumins. Syst Zool. 1969 Sep;18(3):286–295. [PubMed] [Google Scholar]
  33. Sarich V. M., Wilson A. C. Rates of albumin evolution in primates. Proc Natl Acad Sci U S A. 1967 Jul;58(1):142–148. doi: 10.1073/pnas.58.1.142. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Schlesinger M. J., Olsen R. Expression and localization of Escherichia coli alkaline phosphatase synthesized in Salmonella typhimurium cytoplasm. J Bacteriol. 1968 Nov;96(5):1601–1605. doi: 10.1128/jb.96.5.1601-1605.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Singer C. E., Ames B. N. Sunlight ultraviolet and bacterial DNA base ratios. Science. 1970 Nov 20;170(3960):822–825. doi: 10.1126/science.170.3960.822. [DOI] [PubMed] [Google Scholar]
  36. Stanier R. Y., Wachter D., Gasser C., Wilson A. C. Comparative immunological studies of two Pseudomonas enzymes. J Bacteriol. 1970 May;102(2):351–362. doi: 10.1128/jb.102.2.351-362.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Steffen D. L., Cocks G. T., Wilson A. C. Micro-complement fixation in Klebsiella classification. J Bacteriol. 1972 Jun;110(3):803–808. doi: 10.1128/jb.110.3.803-808.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. TORRIANI A. Influence of inorganic phosphate in the formation of phosphatases by Escherichia coli. Biochim Biophys Acta. 1960 Mar 11;38:460–469. doi: 10.1016/0006-3002(60)91281-6. [DOI] [PubMed] [Google Scholar]
  39. WILSON A. C., KAPLAN N. O., LEVINE L., PESCE A., REICHLIN M., ALLISON W. S. EVOLUTION OF LACTIC DEHYDROGENASES. Fed Proc. 1964 Nov-Dec;23:1258–1266. [PubMed] [Google Scholar]
  40. Wallace D. G., Maxson L. R., Wilson A. C. Albumin evolution in frogs: a test of the evolutionary clock hypothesis. Proc Natl Acad Sci U S A. 1971 Dec;68(12):3127–3129. doi: 10.1073/pnas.68.12.3127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Wilson A. C., Sarich V. M. A molecular time scale for human evolution. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1088–1093. doi: 10.1073/pnas.63.4.1088. [DOI] [PMC free article] [PubMed] [Google Scholar]

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