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Biophysical Studies of Interaction between Mycobacterial SepF and FtsZ

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Biophysical Studies of Interaction between Mycobacterial SepF and FtsZ
 
Creator Choudhury, Jagrity
Singh, Lucky
Chaudhuri, Barnali
 
Subject QR Microbiology
 
Description FtsZ is the bacterial tubulin homolog that forms Z-ring, which is a dynamic ring
like structure, at the site of cell division to assemble the divisome and generate
constrictive force for septum formation. SepF is the key protein that anchors the
constricting Z-ring to the protruding septal membrane in Mycobacterium tuberculosis, via its interaction with the intrinsically disordered C-terminal tail of
FtsZ. We characterized the cytosolic component of mycobacterial SepF, and
its interaction with cognate FtsZ, using negative stained electron microscopy,
small angle X-ray scattering, 90 degree angle light scattering and isothermal
titration calorimetry. Cytoplasmic domain of SepF from M. tuberculosis, like
its other homologs, form large ring-shaped polymer. interaction between the
C-terminal part of FtsZ and cytoplasmic SepF was confirmed by isothermal
titration calorimetry. SepF induces bundling of FtsZ in the presence of nucleotides. Our results are discussed in light of the present understanding of divisome assembling
 
Publisher Cell Press
 
Date 2021-02-12
 
Type Article
PeerReviewed
 
Relation https://www.cell.com/biophysj/pdf/S0006-3495(20)31304-7.pdf
http://crdd.osdd.net/open/2667/
 
Identifier Choudhury, Jagrity and Singh, Lucky and Chaudhuri, Barnali (2021) Biophysical Studies of Interaction between Mycobacterial SepF and FtsZ. BIOPHYSICAL JOURNAL, 120 (3). 22A. ISSN 1542-0086