Open AccessSequence and expression of the Mycobacterium leprae dnaJ gene
Author(s) -
Suzanna S. Harvey,
K R McKenzie,
Paul Roche,
Warwick J. Britton
Publication year - 1993
Publication title -
journal of general microbiology/journal of general microbiology
Language(s) - English
Resource type - Journals
eISSN - 2059-9323
pISSN - 0022-1287
DOI - 10.1099/00221287-139-9-2003
Subject(s) - mycobacterium leprae , gene , biology , peptide sequence , open reading frame , homology (biology) , sequence analysis , nucleic acid sequence , heat shock protein , molecular cloning , recombinant dna , genetics , microbiology and biotechnology , molecular mass , biochemistry , leprosy , enzyme , immunology
Study of Mycobacterium leprae, the causative agent of leprosy, has been advanced by the isolation of genes encoding mycobacterial proteins including dnaK encoding the M. leprae 70 kDa heat shock protein. The sequence downstream from dnaK revealed a second open reading frame coding for a protein of 389 amino acids with a calculated molecular mass of 41.2 kDa. Sequence analysis demonstrated significant DNA homology with the dnaJ gene of other organisms. High amino acid sequence identity was obtained between the DnaJ protein of M. leprae and M. tuberculosis (89%) with significant divergence between the two occurring only at the C-terminal end. The expressed recombinant DnaJ protein had a molecular mass of 42 kDa.