Cell division control in Caulobacter crescentus

Biphasic growth dynamics during Caulobacter crescentus division

Shiladitya Banerjee,1, 2, 3 Klevin Lo,1, 4 Matthew K. Daddysman,4 Alan Selewa,4, 5 Thomas Kuntz,6 Aaron R. Dinner,1, 4, 6, ∗ and Norbert F. Scherer1, 4, 6, ∗ 1James Franck Institute, The University of Chicago, Chicago IL 60637, USA 2Department of Physics and Astronomy, University College London, London WC1E 6BT, UK 3Institute for the Physics of Living Systems, University College London, London ...

Caulobacter crescentus

shaped by their activity — both intrinsic and environment induced — and how these networks support the brain computations that underlie externally observable behavior. The second major challenge facing our young field will be applying the basic discoveries we are making to important real-world issues. It is a widely held view that understanding the brain bases of cognitive and behavioral develo...

Characterization of A Novel Mechanism for Cell Division Inhibition in Caulobacter crescentus

Regulation of late flagellar gene transcription and cell division by flagellum assembly in Caulobacter crescentus.

Biogenesis of the single polar flagellum of Caulobacter crescentus is regulated by a complex interplay of cell cycle events and the progression of flagellum assembly. The expression of class III/IV flagellar genes requires the assembly of an early flagellar basal body structure, encoded by class II genes, and is activated by the transcription factor FlbD. Previous experiments indicated that the...

DipM, a new factor required for peptidoglycan remodelling during cell division in Caulobacter crescentus.

In bacteria, cytokinesis is dependent on lytic enzymes that facilitate remodelling of the cell wall during constriction. In this work, we identify a thus far uncharacterized periplasmic protein, DipM, that is required for cell division and polarity in Caulobacter crescentus. DipM is composed of four peptidoglycan binding (LysM) domains and a C-terminal lysostaphin-like (LytM) peptidase domain. ...