This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Garbe, T Articles by Young, D Search for Related Content PubMed PubMed Citation Articles by Garbe, T Articles by Young, D

 Previous Article  |  Next Article 

J Bacteriol. 1990 December; 172(12): 6774-6782

research-article

Cloning and characterization of the aroA gene from Mycobacterium tuberculosis.

Medical Research Council Tuberculosis and Related Infections Unit, Royal Postgraduate Medical School, Hammersmith Hospital, London, United Kingdom.

ABSTRACT

The aroA gene from Mycobacterium tuberculosis has been cloned by complementation of an aroA mutant of Escherichia coli after lysogenization with a recombinant DNA library in the lambda gt11 vector. Detailed characterization of the M. tuberculosis aroA gene by nucleotide sequencing and by immunochemical analysis of the expressed product indicates that it encodes a 5-enolpyruvylshikimate-3-phosphate synthase that is structurally related to analogous enzymes from other bacterial, fungal, and plant sources. The potential use of the cloned gene in construction of genetically defined mutant strains of M. tuberculosis by gene replacement is proposed as a novel approach to the rational attenuation of mycobacterial pathogens and the possible development of new antimycobacterial vaccines.

This article has been cited by other articles:

• Parish, T., Stoker, N. G. (2002). The common aromatic amino acid biosynthesis pathway is essential in Mycobacterium tuberculosis. Microbiology 148: 3069-3077 [Abstract] [Full Text]  
• Hsieh, P.-C., Shenoy, B. C., Samols, D., Phillips, N. F. B. (1996). Cloning, Expression, and Characterization of Polyphosphate Glucokinase from Mycobacterium tuberculosis. J. Biol. Chem. 271: 4909-4915 [Abstract] [Full Text]