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

J Bacteriol. 1994 May;176(9):2525-31. doi: 10.1128/jb.176.9.2525-2531.1994.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyl-CoA Carboxylase / genetics*
  • Amino Acid Sequence
  • Base Sequence
  • Biotin / analysis
  • Carrier Proteins / genetics*
  • DNA Probes
  • Fatty Acid Synthase, Type II
  • Genes, Bacterial / genetics*
  • Lipids / biosynthesis*
  • Molecular Sequence Data
  • Mycobacterium leprae / genetics*
  • Mycobacterium tuberculosis / genetics*
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid

Substances

  • Carrier Proteins
  • DNA Probes
  • Lipids
  • Biotin
  • Fatty Acid Synthase, Type II
  • Acetyl-CoA Carboxylase
  • biotin carboxyl carrier protein

Associated data

  • GENBANK/X63470
  • GENBANK/Z19549