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. 1986 Mar;165(3):911–917. doi: 10.1128/jb.165.3.911-917.1986

Genetic and biochemical characterization of an Escherichia coli K-12 mutant deficient in acyl-coenzyme A thioesterase II.

M L Narasimhan, J L Lampi, J E Cronan Jr
PMCID: PMC214515  PMID: 2869026

Abstract

Mutants of Escherichia coli deficient in thioesterase II activity were isolated by taking advantage of the fact that thioesterase I specifically hydrolyzes long-chain (C12 to C18) acyl coenzyme A (CoA) esters but is unable to cleave the short-chain substrate decanoyl-CoA. One of these lesions (designated tesB1) reduces thioesterase II activity to about 10% of the normal level. The mutant enzyme activity was abnormally labile to temperature, but it was normal in all the other characteristics examined (pH optimum, Km for decanoyl-CoA, molecular weight). The level of thioesterase I activity was unaffected by the tesB1 lesion. The tesB locus was mapped with a closely linked Tn10 insertion. tesB was mapped to minute 10 of the E. coli linkage map, close to the lon locus. The clockwise gene order is lon tesB acrA dnaZ. The tesB mutation is recessive. We found no phenotype for the mutation. The fatty acid compositions of the phospholipids, lipid A, and lipoprotein components are normal in thioesterase II mutants. These data show that thioesterases I and II of E. coli are encoded by different genetic loci and strongly suggest that tesB is the structural gene for thioesterase II.

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Selected References

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  1. BLIGH E. G., DYER W. J. A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959 Aug;37(8):911–917. doi: 10.1139/o59-099. [DOI] [PubMed] [Google Scholar]
  2. Bachmann B. J. Linkage map of Escherichia coli K-12, edition 7. Microbiol Rev. 1983 Jun;47(2):180–230. doi: 10.1128/mr.47.2.180-230.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Barnes E. M., Jr Long-chain fatty acyl thioesterases I and II from Escherichia coli. Methods Enzymol. 1975;35:102–109. doi: 10.1016/0076-6879(75)35144-6. [DOI] [PubMed] [Google Scholar]
  4. Barnes E. M., Jr, Wakil S. J. Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase. J Biol Chem. 1968 Jun 10;243(11):2955–2962. [PubMed] [Google Scholar]
  5. Barnes E. M., Jr, Wakil S. J., Swindell A. C. Purification and properties of a palmityl thioesterase II from Escherichia coli. J Biol Chem. 1970 Jun;245(12):3122–3128. [PubMed] [Google Scholar]
  6. Bonner W. M., Bloch K. Purification and properties of fatty acyl thioesterase I from Escherichia coli. J Biol Chem. 1972 May 25;247(10):3123–3133. [PubMed] [Google Scholar]
  7. Byers D., Meighen E. Purification and characterization of a bioluminescence-related fatty acyl esterase from Vibrio harveyi. J Biol Chem. 1985 Jun 10;260(11):6938–6944. [PubMed] [Google Scholar]
  8. Chang Y. Y., Cronan J. E., Jr Mapping nonselectable genes of Escherichia coli by using transposon Tn10: location of a gene affecting pyruvate oxidase. J Bacteriol. 1982 Sep;151(3):1279–1289. doi: 10.1128/jb.151.3.1279-1289.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Cheesbrough T. M., Kolattukudy P. E. Purification and characterization of a fatty acyl-CoA hydrolase from the uropygial glands of Peking ducks (Anas domesticus). Arch Biochem Biophys. 1985 Feb 15;237(1):208–216. doi: 10.1016/0003-9861(85)90271-1. [DOI] [PubMed] [Google Scholar]
  10. Coleman W. G., Jr, Leive L. Two mutations which affect the barrier function of the Escherichia coli K-12 outer membrane. J Bacteriol. 1979 Sep;139(3):899–910. doi: 10.1128/jb.139.3.899-910.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Crabtree S., Cronan J. E., Jr Facile and gentle method for quantitative lysis of Escherichia coli and Salmonella typhimurium. J Bacteriol. 1984 Apr;158(1):354–356. doi: 10.1128/jb.158.1.354-356.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Cronan J. E., Jr, Silbert D. F., Wulff D. L. Mapping of the fabA locus for unsaturated fatty acid biosynthesis in Escherichia coli. J Bacteriol. 1972 Oct;112(1):206–211. doi: 10.1128/jb.112.1.206-211.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. GOLDMAN P., VAGELOS P. R. The specificity of triglyceride synthesis from diglycerides in chicken adipose tissue. J Biol Chem. 1961 Oct;236:2620–2623. [PubMed] [Google Scholar]
  14. Garrett J., Fusselman R., Hise J., Chiou L., Smith-Grillo D., Schulz J., Young R. Cell lysis by induction of cloned lambda lysis genes. Mol Gen Genet. 1981;182(2):326–331. doi: 10.1007/BF00269678. [DOI] [PubMed] [Google Scholar]
  15. Hirashima A., Wu H. C., Venkateswaran P. S., Inouye M. Two forms of a structural lipoprotein in the envelope of Escherichia coli. Further characterization of the free form. J Biol Chem. 1973 Aug 25;248(16):5654–5659. [PubMed] [Google Scholar]
  16. Larson J. D., Kolattukudy P. E. Isolation and characterization of an acyl-CoA thioesterase from dark-grown Euglena gracilis. Arch Biochem Biophys. 1985 Feb 15;237(1):27–37. doi: 10.1016/0003-9861(85)90250-4. [DOI] [PubMed] [Google Scholar]
  17. Low K. B. Escherichia coli K-12 F-prime factors, old and new. Bacteriol Rev. 1972 Dec;36(4):587–607. doi: 10.1128/br.36.4.587-607.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Maloy S. R., Nunn W. D. Selection for loss of tetracycline resistance by Escherichia coli. J Bacteriol. 1981 Feb;145(2):1110–1111. doi: 10.1128/jb.145.2.1110-1111.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Murphy D. J., Mukherjee K. D., Latzko E., Woodrow I. E. Solubilization, purification and kinetic properties of three membrane-bound long-chain acyl-coenzyme-A thioesterases from microsomes of photosynthetic tissue. Eur J Biochem. 1984 Jul 2;142(1):43–48. doi: 10.1111/j.1432-1033.1984.tb08248.x. [DOI] [PubMed] [Google Scholar]
  20. Nakamura H. Gene-Controlled Resistance to Acriflavine and Other Basic Dyes in Escherichia coli. J Bacteriol. 1965 Jul;90(1):8–14. doi: 10.1128/jb.90.1.8-14.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Nakamura H., Tojo T., Greenberg J. Interaction of the expression of two membrane genes, acrA and plsA, in Escherichia coli K-12. J Bacteriol. 1975 Jun;122(3):874–879. doi: 10.1128/jb.122.3.874-879.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Rock C. O., Jackowski S. Regulation of phospholipid synthesis in Escherichia coli. Composition of the acyl-acyl carrier protein pool in vivo. J Biol Chem. 1982 Sep 25;257(18):10759–10765. [PubMed] [Google Scholar]
  23. Shine W. E., Mancha M., Stumpf P. K. Fat metabolism in higher plants. The function of acyl thioesterases in the metabolism of acyl-coenzymes A and acyl-acyl carrier proteins. Arch Biochem Biophys. 1976 Jan;172(1):110–116. doi: 10.1016/0003-9861(76)90054-0. [DOI] [PubMed] [Google Scholar]
  24. Spencer A. K., Greenspan A. D., Cronan J. E., Jr Thioesterases I and II of Escherichia coli. Hydrolysis of native acyl-acyl carrier protein thioesters. J Biol Chem. 1978 Sep 10;253(17):5922–5926. [PubMed] [Google Scholar]
  25. Tamaki S., Sato T., Matsuhashi M. Role of lipopolysaccharides in antibiotic resistance and bacteriophage adsorption of Escherichia coli K-12. J Bacteriol. 1971 Mar;105(3):968–975. doi: 10.1128/jb.105.3.968-975.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. Wijsman H. J., Pafort H. C. Pleiotropic mutations in Escherichia coli conferring tolerance to glycine and sensitivity to penicillin. Mol Gen Genet. 1974;128(4):349–357. doi: 10.1007/BF00268522. [DOI] [PubMed] [Google Scholar]
  28. Yem D. W., Wu H. C. Physiological characterization of an Escherichia coli mutant altered in the structure of murein lipoprotein. J Bacteriol. 1978 Mar;133(3):1419–1426. doi: 10.1128/jb.133.3.1419-1426.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]

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