ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

MtFtsX a predicted membrane domain of ABC transporter complex MtFtsEX of Mycobacterium tuberculosis interacts with the cell division protein MtFtsZ

Mir, MA and Srinivasan, R and Ajitkumar, P (2019) MtFtsX a predicted membrane domain of ABC transporter complex MtFtsEX of Mycobacterium tuberculosis interacts with the cell division protein MtFtsZ. In: International Journal of Mycobacteriology, 8 (3). pp. 281-286.

[img]
Preview
PDF
int_jou_myc_8-3_281-286_2019.pdf - Published Version

Download (700kB) | Preview
Official URL: https://doi.org/10.4103/ijmy.ijmy_98_19

Abstract

Background: Bacterial cytokinesis is orchestrated by a complex of dozen of proteins called 'divisome' at the mid-cell site. FtsZ, the eukaryotic tubulin homolog, localizes to the mid-cell site where it polymerizes and forms a cytokinetic Z-ring. The Z-ring acts as a docking platform for other proteins to localize. In model organisms, Escherichia coli and Bacillus subtilis, FtsZ is known to interact with several proteins. The role of few of these interactions is known, while of others is yet to be studied. In Mycobacterium tuberculosis, the cell division and its regulation are poorly studied. Although, most of the divisome proteins are conserved in M. tuberculosis, surprisingly the homologues of the protein factors required for membrane association of Z-ring and its stabilization are absent. In E. coli FtsE and FtsX, the constituent ATPase and membrane domains of the ABC transporter complex, localize to the Z-ring immediately after Z-ring stabilizing proteins, ZipA and FtsA. Therefore, investigation of the interaction between MtFtsX and MtFtsZ is demanding. Methods: Bacterial two-hybrid system was used to identify the interaction between MtFtsE and MtFtsZ. This interaction was further confirmed by biochemical methods of Ni2+-NTA agarose pull-down and coimmunoprecipitation. Results and Conclusion: Here, we demonstrated that MtFtsX interacts with MtFtsZ in vivo and ex-vivo. Further, we showed that self-interacting MtFtsX interacts with MtFtsE. However, we did not find any interaction between MtFtsE and MtFtsZ. These results suggest that the membrane domain MtFtsX of the ABC transporter complex 'MtFtsEX' might be the membrane-tethering and stabilizing factor for Z-ring in M. tuberculosis.

Item Type: Journal Article
Publication: International Journal of Mycobacteriology
Publisher: Wolters Kluwer Medknow Publications
Additional Information: The copyright for this article belongs to the Authors.
Keywords: ABC transporter; bacterial protein; FtsA protein; FtsX protein; FtsZ protein; unclassified drug; ZipA protein; bacterial protein; cell cycle protein; cytoskeleton protein; FtsX protein, bacteria; FtsZ protein, Bacteria; protein binding, amino terminal sequence; Article; Bacillus subtilis; carboxy terminal sequence; cell cycle regulation; cell division; chromatin immunoprecipitation; controlled study; cytokinesis; Escherichia coli; in vivo study; Mycobacterium tuberculosis; nonhuman; predictive value; priority journal; protein domain; protein expression; protein function; protein localization; protein protein interaction; cell division; genetics; metabolism; Mycobacterium tuberculosis; two hybrid system, Bacterial Proteins; Cell Cycle Proteins; Cell Division; Cytoskeletal Proteins; Mycobacterium tuberculosis; Protein Binding; Two-Hybrid System Techniques
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited: 23 Oct 2022 06:46
Last Modified: 23 Oct 2022 06:46
URI: https://eprints.iisc.ac.in/id/eprint/77504

Actions (login required)

View Item View Item