Identification of a second Mycobacterium tuberculosis gene cluster encoding proteins of an ABC phosphate transporter

Following the identification of a M. tuberculosis phosphate transporter belonging to the superfamily of ABC transporters, we report on the cloning and sequencing of two additional genes, called pstS-3 and pstC-2, encoding proteins homologous to PstS and PstC of Escherichia coli, respectively. Togeth...

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Bibliographic Details
Published in:FEBS letters 1996-09, Vol.394 (2), p.206-212
Main Authors: Braibant, Martine, Lefèvre, Philippe, de Wit, Lucas, Ooms, Josette, Peirs, Priska, Huygen, Kris, Wattiez, Rudy, Content, Jean
Format: Article
Language:English
Subjects:
Ag 88
Amino Acid Sequence
ATP-Binding Cassette Transporters - chemistry
ATP-Binding Cassette Transporters - genetics
ATP-binding-cassette transporter
Bacterial Proteins
Base Sequence
Binding Sites
Carrier Proteins - chemistry
Carrier Proteins - genetics
Cloning, Molecular
Conserved Sequence
Cyanogen Bromide
Electrophoresis, Polyacrylamide Gel
Genes, Bacterial
Immunoblotting
Molecular Sequence Data
Multigene Family
Mycobacterium tuberculosis
Mycobacterium tuberculosis - chemistry
Mycobacterium tuberculosis - genetics
Operon
Peptides - chemistry
Phosphate transport
Phosphate-Binding Proteins
PstC
PstS
Sequence Analysis, DNA
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Summary:Following the identification of a M. tuberculosis phosphate transporter belonging to the superfamily of ABC transporters, we report on the cloning and sequencing of two additional genes, called pstS-3 and pstC-2, encoding proteins homologous to PstS and PstC of Escherichia coli, respectively. Together with the previously isolated M. tuberculosis gene similar to the E. coli pstA, these are included in a cluster encoding a second putative phosphate transport system. We demonstrate that pstS-3 encodes the previously described Ag 88, a 40 kDa M. bovis BCG culture filtrate antigen (immunodominant in H-2 b haplotype type mice). Finally, a signature motif identifying integral transmembrane proteins of prokaryotic phosphate binding-dependent permeases is proposed.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(96)00953-2