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. 1994 May;176(9):2525–2531. doi: 10.1128/jb.176.9.2525-2531.1994

Lipid synthesis in mycobacteria: characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis.

E Norman 1, K A De Smet 1, N G Stoker 1, C Ratledge 1, P R Wheeler 1, J W Dale 1
PMCID: PMC205389  PMID: 7909542

Abstract

The causative agents of leprosy and tuberculosis, Mycobacterium leprae and Mycobacterium tuberculosis, have a lipid-rich cell envelope which contributes to virulence and antibiotic resistance. Acyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis, consists in mycobacteria of two subunits, one of which is biotinylated. Genes from M. leprae and M. tuberculosis encoding a biotinylated protein have been cloned and sequenced. Analysis of the derived protein sequences demonstrated the presence of biotin-binding sites and putative ATP-bicarbonate interactions sites, consistent with the proteins having a biotin carboxylase function as well as their being biotin carrier proteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Alix J. H. A rapid procedure for cloning genes from lambda libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome. DNA. 1989 Dec;8(10):779–789. doi: 10.1089/dna.1989.8.779. [DOI] [PubMed] [Google Scholar]
  2. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  3. Browner M. F., Taroni F., Sztul E., Rosenberg L. E. Sequence analysis, biogenesis, and mitochondrial import of the alpha-subunit of rat liver propionyl-CoA carboxylase. J Biol Chem. 1989 Jul 25;264(21):12680–12685. [PubMed] [Google Scholar]
  4. Cronan J. E., Jr Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins. J Biol Chem. 1990 Jun 25;265(18):10327–10333. [PubMed] [Google Scholar]
  5. Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fall R. R., Vagelos P. R. Biotin carboxyl carrier protein from Escherichia coli. Methods Enzymol. 1975;35:17–25. doi: 10.1016/0076-6879(75)35133-1. [DOI] [PubMed] [Google Scholar]
  7. Gornicki P., Scappino L. A., Haselkorn R. Genes for two subunits of acetyl coenzyme A carboxylase of Anabaena sp. strain PCC 7120: biotin carboxylase and biotin carboxyl carrier protein. J Bacteriol. 1993 Aug;175(16):5268–5272. doi: 10.1128/jb.175.16.5268-5272.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Haase F. C., Henrikson K. P., Treble D. H., Allen S. H. The subunit structure and function of the propionyl coenzyme A carboxylase of Mycobacterium smegmatis. J Biol Chem. 1982 Oct 25;257(20):11994–11999. [PubMed] [Google Scholar]
  9. Henrikson K. P., Allen S. H. Purification and subunit structure of propionyl coenzyme A carboxylase of Mycobacterium smegmatis. J Biol Chem. 1979 Jul 10;254(13):5888–5891. [PubMed] [Google Scholar]
  10. Higgins D. G., Sharp P. M. CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene. 1988 Dec 15;73(1):237–244. doi: 10.1016/0378-1119(88)90330-7. [DOI] [PubMed] [Google Scholar]
  11. Higgins D. G., Sharp P. M. Fast and sensitive multiple sequence alignments on a microcomputer. Comput Appl Biosci. 1989 Apr;5(2):151–153. doi: 10.1093/bioinformatics/5.2.151. [DOI] [PubMed] [Google Scholar]
  12. Knowles J. R. The mechanism of biotin-dependent enzymes. Annu Rev Biochem. 1989;58:195–221. doi: 10.1146/annurev.bi.58.070189.001211. [DOI] [PubMed] [Google Scholar]
  13. Lamhonwah A. M., Mahuran D., Gravel R. A. Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro- and mature alpha chains in the deduced primary sequence of a full-length cDNA. Nucleic Acids Res. 1989 Jun 12;17(11):4396–4396. doi: 10.1093/nar/17.11.4396. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lamhonwah A. M., Quan F., Gravel R. A. Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631–636. doi: 10.1016/0003-9861(87)90146-9. [DOI] [PubMed] [Google Scholar]
  15. Li S. J., Cronan J. E., Jr The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J Biol Chem. 1992 Jan 15;267(2):855–863. [PubMed] [Google Scholar]
  16. Lim F., Morris C. P., Occhiodoro F., Wallace J. C. Sequence and domain structure of yeast pyruvate carboxylase. J Biol Chem. 1988 Aug 15;263(23):11493–11497. [PubMed] [Google Scholar]
  17. Lyons J., Sinos C., Destree A., Caiazzo T., Havican K., McKenzie S., Panicali D., Mahr A. Expression of Mycobacterium tuberculosis and Mycobacterium leprae proteins by vaccinia virus. Infect Immun. 1990 Dec;58(12):4089–4098. doi: 10.1128/iai.58.12.4089-4098.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. López-Casillas F., Bai D. H., Luo X. C., Kong I. S., Hermodson M. A., Kim K. H. Structure of the coding sequence and primary amino acid sequence of acetyl-coenzyme A carboxylase. Proc Natl Acad Sci U S A. 1988 Aug;85(16):5784–5788. doi: 10.1073/pnas.85.16.5784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Minnikin D. E., Dobson G., Goodfellow M., Magnusson M., Ridell M. Distribution of some mycobacterial waxes based on the phthiocerol family. J Gen Microbiol. 1985 Jun;131(6):1375–1381. doi: 10.1099/00221287-131-6-1375. [DOI] [PubMed] [Google Scholar]
  20. Muramatsu S., Mizuno T. Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli. Nucleic Acids Res. 1989 May 25;17(10):3982–3982. doi: 10.1093/nar/17.10.3982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Murtif V. L., Samols D. Mutagenesis affecting the carboxyl terminus of the biotinyl subunit of transcarboxylase. Effects on biotination. J Biol Chem. 1987 Aug 25;262(24):11813–11816. [PubMed] [Google Scholar]
  22. Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444–2448. doi: 10.1073/pnas.85.8.2444. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Rainwater D. L., Kolattukudy P. E. Isolation and characterization of acyl coenzyme A carboxylases from Mycobacterium tuberculosis and Mycobacterium bovis, which produce multiple methyl-branched mycocerosic acids. J Bacteriol. 1982 Aug;151(2):905–911. doi: 10.1128/jb.151.2.905-911.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Saiki R. K., Gelfand D. H., Stoffel S., Scharf S. J., Higuchi R., Horn G. T., Mullis K. B., Erlich H. A. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science. 1988 Jan 29;239(4839):487–491. doi: 10.1126/science.2448875. [DOI] [PubMed] [Google Scholar]
  25. Samols D., Thornton C. G., Murtif V. L., Kumar G. K., Haase F. C., Wood H. G. Evolutionary conservation among biotin enzymes. J Biol Chem. 1988 May 15;263(14):6461–6464. [PubMed] [Google Scholar]
  26. Takai T., Yokoyama C., Wada K., Tanabe T. Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence. J Biol Chem. 1988 Feb 25;263(6):2651–2657. [PubMed] [Google Scholar]
  27. Tuberculosis and leprosy. Br Med Bull. 1988 Jul;44(3):523–820. [PubMed] [Google Scholar]
  28. Vega-López F., Brooks L. A., Dockrell H. M., De Smet K. A., Thompson J. K., Hussain R., Stoker N. G. Sequence and immunological characterization of a serine-rich antigen from Mycobacterium leprae. Infect Immun. 1993 May;61(5):2145–2153. doi: 10.1128/iai.61.5.2145-2153.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Wheeler P. R., Bulmer K., Ratledge C., Dale J. W., Norman E. Control of acyl-CoA carboxylase activity in mycobacteria. FEMS Microbiol Lett. 1992 Jan 1;69(2):169–172. doi: 10.1016/0378-1097(92)90623-v. [DOI] [PubMed] [Google Scholar]
  30. Young R. A., Mehra V., Sweetser D., Buchanan T., Clark-Curtiss J., Davis R. W., Bloom B. R. Genes for the major protein antigens of the leprosy parasite Mycobacterium leprae. Nature. 1985 Aug 1;316(6027):450–452. doi: 10.1038/316450a0. [DOI] [PubMed] [Google Scholar]
  31. Zainuddin Z. F., Dale J. W. Polymorphic repetitive DNA sequences in Mycobacterium tuberculosis detected with a gene probe from a Mycobacterium fortuitum plasmid. J Gen Microbiol. 1989 Sep;135(9):2347–2355. doi: 10.1099/00221287-135-9-2347. [DOI] [PubMed] [Google Scholar]

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