FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one

HP Erickson, DE Anderson… - … and molecular biology …, 2010 - Am Soc Microbiol
FtsZ, a bacterial homolog of tubulin, is well established as forming the cytoskeletal
framework for the cytokinetic ring. Recent work has shown that purified FtsZ, in the absence …

Targeting the assembly of bacterial cell division protein FtsZ with small molecules

C Schaffner-Barbero, M Martín-Fontecha… - ACS chemical …, 2012 - ACS Publications
FtsZ is the key protein of bacterial cell division and an emergent target for new antibiotics. It
is a filament-forming GTPase and a structural homologue of eukaryotic tubulin. A number of …

Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus

T Matsui, J Yamane, N Mogi, H Yamaguchi… - … Section D: Biological …, 2012 - scripts.iucr.org
FtsZ is a key molecule in bacterial cell division. In the presence of GTP, it polymerizes into
tubulin-like protofilaments by head-to-tail association. Protofilaments of FtsZ seem to adopt a …

A polymerization-associated structural switch in FtsZ that enables treadmilling of model filaments

JM Wagstaff, M Tsim, MA Oliva, A García-Sanchez… - MBio, 2017 - Am Soc Microbiol
Bacterial cell division in many organisms involves a constricting cytokinetic ring that is
orchestrated by the tubulin-like protein FtsZ. FtsZ forms dynamic filaments close to the …

A flexible C‐terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivo

PJ Buske, PA Levin - Molecular microbiology, 2013 - Wiley Online Library
Assembly of the cytoskeletal protein FtsZ into a ring‐like structure is required for bacterial
cell division. Structurally, FtsZ consists of four domains: the globular N‐terminal core, a …

Recent progress of bacterial FtsZ inhibitors with a focus on peptides

H Han, Z Wang, T Li, D Teng, R Mao, Y Hao… - The FEBS …, 2021 - Wiley Online Library
In recent years, the rise of antibiotic resistance has become a primary health problem. With
the emergence of bacterial resistance, the need to explore and develop novel antibacterial …

Halogenation of tyrosine perturbs large-scale protein self-organization

H Sun, H Jia, O Kendall, J Dragelj, V Kubyshkin… - Nature …, 2022 - nature.com
Protein halogenation is a common non-enzymatic post-translational modification
contributing to aging, oxidative stress-related diseases and cancer. Here, we report a …

Multiple effects of benzamide antibiotics on FtsZ function

DW Adams, LJ Wu, LG Czaplewski… - Molecular …, 2011 - Wiley Online Library
Cell division in almost all bacteria is orchestrated by the essential tubulin homologue FtsZ,
which assembles into a ring‐like structure and acts as a scaffold for the division machinery …

Structural change in FtsZ Induced by intermolecular interactions between bound GTP and the T7 loop

T Matsui, X Han, J Yu, M Yao, I Tanaka - Journal of Biological Chemistry, 2014 - ASBMB
FtsZ is a prokaryotic homolog of tubulin and is a key molecule in bacterial cell division. FtsZ
with bound GTP polymerizes into tubulin-like protofilaments. Upon polymerization, the T7 …

Synthetic inhibitors of bacterial cell division targeting the GTP-binding site of FtsZ

LB Ruiz-Avila, S Huecas, M Artola… - ACS chemical …, 2013 - ACS Publications
Cell division protein FtsZ is the organizer of the cytokinetic Z-ring in most bacteria and a
target for new antibiotics. FtsZ assembles with GTP into filaments that hydrolyze the …