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primary topic: Biophysical Studies of Interaction between Mycobacterial SepF and FtsZ

Biophysical Studies of Interaction between Mycobacterial SepF and FtsZ
type: AcademicArticle
type: Article
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
volume: 120
issue: 3
is part of: BIOPHYSICAL JOURNAL
status: peerReviewed
status: published
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository
subject: QR Microbiology

Cell Press
type: Organization

BIOPHYSICAL JOURNAL
type: Collection
issn: 15420086

Jagrity Choudhury
type: Person
given name: Jagrity
family name: Choudhury

Barnali Chaudhuri
type: Person
given name: Barnali
family name: Chaudhuri

Lucky Singh
type: Person
given name: Lucky
family name: Singh

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primary topic: Biophysical Studies of Interaction between Mycobacterial SepF and FtsZ

QR Microbiology
type: Concept