In silico identification and characterization of the ion transport specificity for P-type ATPases in the Mycobacterium tuberculosis complex

BMC Structural Biology

Carlos-Yesid Soto²  Leonardo Mariño-Ramírez¹  David Landsman³  Luz-Mary Salazar²  Jenifer Cuesta-Bernal²  Miyer Patiño-Ruiz²  Andrés León-Torres²  Lorena Novoa-Aponte² 

[1] PanAmerican Bioinformatics Institute, Santa Marta, Magdalena, Colombia;Chemistry Department, Faculty of Sciences, Universidad Nacional de Colombia, Bogotá, Colombia, Carrera 30 # 45–03, Ciudad Universitaria, Bogotá, Colombia;Computational Biology Branch, NCBI, NLM, NIH, Bethesda, USA

关键词: Conserved motifs;    Ion transport;    P-type ATPases;    Mycobacterium tuberculosis complex;    Tuberculosis;   

Others  :  1118610
DOI  :  10.1186/1472-6807-12-25

 received in 2012-06-25, accepted in 2012-09-27,  发布年份 2012

【 摘 要 】

Background

P-type ATPases hydrolyze ATP and release energy that is used in the transport of ions against electrochemical gradients across plasma membranes, making these proteins essential for cell viability. Currently, the distribution and function of these ion transporters in mycobacteria are poorly understood.

Results

In this study, probabilistic profiles were constructed based on hidden Markov models to identify and classify P-type ATPases in the Mycobacterium tuberculosis complex (MTBC) according to the type of ion transported across the plasma membrane. Topology, hydrophobicity profiles and conserved motifs were analyzed to correlate amino acid sequences of P-type ATPases and ion transport specificity. Twelve candidate P-type ATPases annotated in the M. tuberculosis H37Rv proteome were identified in all members of the MTBC, and probabilistic profiles classified them into one of the following three groups: heavy metal cation transporters, alkaline and alkaline earth metal cation transporters, and the beta subunit of a prokaryotic potassium pump. Interestingly, counterparts of the non-catalytic beta subunits of Hydrogen/Potassium and Sodium/Potassium P-type ATPases were not found.

Conclusions

The high content of heavy metal transporters found in the MTBC suggests that they could play an important role in the ability of M. tuberculosis to survive inside macrophages, where tubercle bacilli face high levels of toxic metals. Finally, the results obtained in this work provide a starting point for experimental studies that may elucidate the ion specificity of the MTBC P-type ATPases and their role in mycobacterial infections.

【 授权许可】

   
2012 Novoa-Aponte et al.; licensee BioMed Central Ltd.

【 图 表 】

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