creators_name: Choudhury, Jagrity
creators_name: Singh, Lucky
creators_name: Chaudhuri, Barnali
type: article
datestamp: 2021-04-26 05:54:59
lastmod: 2021-04-26 05:54:59
metadata_visibility: show
title: Biophysical Studies of Interaction between Mycobacterial SepF and FtsZ
ispublished: pub
subjects: QR
note: Meeting Abstract 
abstract: 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
date: 2021-02-12
date_type: published
publication: BIOPHYSICAL JOURNAL
volume: 120
number: 3
publisher: Cell Press
pagerange: 22A
refereed: TRUE
issn: 1542-0086
official_url: https://www.cell.com/biophysj/pdf/S0006-3495(20)31304-7.pdf
citation:   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