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Jordan M. Barrows

As seen in: BioRxiv
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Articles

The Cell Division Protein FzlA Performs a Conserved Function in Diverse Alphaproteobacteria

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By Isaac Payne, Jordan M. Barrows, Pamela Brown Verified, Brody Aubry
| BioRxiv
Abstract In almost all bacteria, the tubulin-like GTPase FtsZ polymerizes to form a Z-ring that marks the site of division. FtsZ recruits other proteins, collectively known as the divisome, that together remodel and constrict the envelope. Constriction is driven by peptidoglycan (PG) cell wall synthesis by the glycosyltransferase FtsW and the transpeptidase FtsI (FtsWI), but these enzymes require activation to function.
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Intrinsic and extrinsic factors regulate FtsZ function in Caulobacter crescentus

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By Jordan M. Barrows, Ashley Anderson, Erin D Goley, Barbara K Talavera-Figueroa
| BioRxiv
Abstract Bacterial cell division is crucial for replication and requires careful coordination via a complex set of proteins collectively known as the divisome. The tubulin-like GTPase FtsZ is the master regulator of this process and serves to recruit downstream divisome proteins and regulate their activities. Upon arrival at mid-cell, FtsZ associates with the membrane via anchoring proteins and exhibits treadmilling motion, driven by its GTP binding and hydrolysis activities.
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FtsA Regulates Z-Ring Morphology and Cell Wall Metabolism in an FtsZ C-Terminal Linker-Dependent Manner in Caulobacter crescentus

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By Jordan M. Barrows, Kousik Sundararajan, Anant Bhargava, Erin D Goley
| asm.org
Research Article Jordan M. Barrows, Kousik Sundararajan, Anant Bhargava, Erin D. Goley Conrad W. Mullineaux, Editor DOI: 10.1128/JB.00693-19 ABSTRACT Bacterial cell division requires the assembly of a multiprotein division machinery, or divisome, that remodels the cell envelope to cause constriction. The cytoskeletal protein FtsZ forms a ringlike scaffold for the divisome at the incipient division site.
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