Paul J. Buske

Washington University in St. Louis

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Petra Anne Levin

Washington University in St. Louis

Rohit V. Pappu

Washington University in St. Louis

Anuradha Mittal

University of Amsterdam

Megan C. Cohan

Washington University in St. Louis

Alex S. Holehouse

Washington University in St. Louis

Steven J. Grigsby

Washington University in St. Louis

Ammon E. Posey

Washington University in St. Louis

Norbert S. Hill

University of California, Berkeley

Jason D. Zuke

University of Wisconsin–Madison

An‐Chun Chien

Washington University in St. Louis

Cooperative Institutions

Washington University in St. Louis

University of Pittsburgh

Centre National de la Recherche Scientifique

Living Systems (United States)

Imperial College London

University of Michigan–Ann Arbor

University of Illinois Urbana-Champaign

AstraZeneca (United States)

Seoul National University

Institute of Molecular Biology and Biophysics

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The C Terminus of FtsZ Regulates FtsZ Assembly Dynamics and Is Required for Bacillus subtilis Cell Division

Paul J. Buske

FtsZ

10.7936/k7668b61

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Citations (0)

Sequence-Encoded Charge Patterning of the Intrinsically Disordered Tail of FtsZ Impacts Polymerization and Bacterial Cell Division

Biophysical Journal (2018)

Megan C. Cohan Ammon E. Posey Anuradha Mittal Steven J. Grigsby Alex S. Holehouse

FtsZ

Division ring

Conserved sequence

10.1016/j.bpj.2017.11.3226

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A nutrient-dependent division antagonist is regulated post-translationally by the Clp proteases in Bacillus subtilis

BMC Microbiology (2018)

Norbert S. Hill Jason D. Zuke Paul J. Buske An‐Chun Chien Petra Anne Levin

Changes in nutrient availability have dramatic and well-defined impacts on both transcription and translation in bacterial cells. At the same time, the role of post-translational control in adaptation to nutrient-poor environments is poorly understood. Previous studies demonstrate the ability of the glucosyltransferase UgtP to influence cell size in response to nutrient availability. Under nutrient-rich medium, interactions with its substrate UDP-glucose promote interactions between UgtP and the tubulin-like cell division protein FtsZ in Bacillus subtilis, inhibiting maturation of the cytokinetic ring and increasing cell size. In nutrient-poor medium, reductions in UDP-glucose availability favor UgtP oligomerization, sequestering it from FtsZ and allowing division to occur at a smaller cell mass. Intriguingly, in nutrient-poor conditions UgtP levels are reduced ~ 3-fold independent of UDP-glucose. B. subtilis cells cultured under different nutrient conditions indicate that UgtP accumulation is controlled through a nutrient-dependent post-translational mechanism dependent on the Clp proteases. Notably, all three B. subtilis Clp chaperones appeared able to target UgtP for degradation during growth in nutrient-poor conditions. Together these findings highlight conditional proteolysis as a mechanism for bacterial adaptation to a rapidly changing nutritional landscape.

FtsZ

Proteolysis

Cell Physiology

10.1186/s12866-018-1155-2

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Citations (5)

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

Molecular Microbiology (2013)

Paul J. Buske Petra Anne Levin

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 flexible linker, 8-9 conserved residues implicated in interactions with modulatory proteins, and a highly variable set of 4-10 residues at its very C terminus. Largely ignored and distinguished by lack of primary sequence conservation, the linker is presumed to be intrinsically disordered. Here we employ genetics, biochemistry and cytology to dissect the role of the linker in FtsZ function. Data from chimeric FtsZs substituting the native linker with sequences from unrelated FtsZs as well as a helical sequence from human beta-catenin indicate that while variations in the primary sequence are well tolerated, an intrinsically disordered linker is essential for Bacillus subtilis FtsZ assembly. Linker lengths ranging from 25 to 100 residues supported FtsZ assembly, but replacing the B. subtilis FtsZ linker with a 249-residue linker from Agrobacterium tumefaciens FtsZ interfered with cell division. Overall, our results support a model in which the linker acts as a flexible tether allowing FtsZ to associate with the membrane through a conserved C-terminal domain while simultaneously interacting with itself and modulatory proteins in the cytoplasm.

FtsZ

Linker

Conserved sequence

10.1111/mmi.12272

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Citations (110)

Actin‐like protein 1 (ALP1) is a component of dynamic, high molecular weight complexes in Toxoplasma gondii

Cytoskeleton (2009)

Jennifer L. Gordon Jeffrey S. Buguliskis Paul J. Buske L. David Sibley

Apicomplexan parasites, such as Toxoplasma gondii, rely on actin-based motility for cell invasion, yet conventional actin does not appear to be required for cell division in these parasites. Apicomplexans also contain a variety of actin-related proteins (Arps); however, most of these not directly orthologous to Arps in well-studied systems. We recently identified an apicomplexan-specific member of this family called Actin-Like Protein 1, (ALP1), which plays a role in the assembly of vesicular components recruited to the inner membrane complex (IMC) of daughter cells during cell division. In addition to its enrichment at daughter cell membranes, ALP1 is localized throughout the cytoplasm both diffusely distributed and concentrated in clusters that are detected by fluorescence microscopy, suggesting it forms complexes. Using quantitative optical imaging methods, including fluorescence recovery after photobleaching (FRAP) and fluorescence loss in photobleaching (FLIP), we demonstrated that ALP1 is a component of a large complex, and that it readily exchanges between diffusible and complex-bound forms. Sedimentation and density gradient analyses revealed that ALP1 is found in a freely soluble state as well as high molecular weight complexes. During cell division, ALP1 was dynamically associated with the IMC, suggesting it rapidly cycles between freely diffusible and complex forms during daughter cell assembly.

Photobleaching

10.1002/cm.20414

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Citations (18)

Identification of two binding partners for the bacterial actin homolog MreB

Paul J. Buske

MreB

Identification

Source

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Citations (0)

The Intrinsically Disordered Tail of FtsZ Impacts Polymerization and Bacterial Cell Division Through Sequence-Encoded Charge Patterning

Biophysical Journal (2017)

Megan C. Cohan Ammon E. Posey Steven J. Grigsby Alex S. Holehouse Anuradha Mittal

FtsZ

Sequence (biology)

Linker

CTL*

10.1016/j.bpj.2016.11.2760

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A Moonlighting Enzyme Links Escherichia coli Cell Size with Central Metabolism

PLoS Genetics (2013)

Norbert S. Hill Paul J. Buske Yue Shi Petra Anne Levin

Growth rate and nutrient availability are the primary determinants of size in single-celled organisms: rapidly growing Escherichia coli cells are more than twice as large as their slow growing counterparts. Here we report the identification of the glucosyltransferase OpgH as a nutrient-dependent regulator of E. coli cell size. During growth under nutrient-rich conditions, OpgH localizes to the nascent septal site, where it antagonizes assembly of the tubulin-like cell division protein FtsZ, delaying division and increasing cell size. Biochemical analysis is consistent with OpgH sequestering FtsZ from growing polymers. OpgH is functionally analogous to UgtP, a Bacillus subtilis glucosyltransferase that inhibits cell division in a growth rate-dependent fashion. In a striking example of convergent evolution, OpgH and UgtP share no homology, have distinct enzymatic activities, and appear to inhibit FtsZ assembly through different mechanisms. Comparative analysis of E. coli and B. subtilis reveals conserved aspects of growth rate regulation and cell size control that are likely to be broadly applicable. These include the conservation of uridine diphosphate glucose as a proxy for nutrient status and the use of moonlighting enzymes to couple growth rate-dependent phenomena to central metabolism.

FtsZ

Glucosyltransferases

10.1371/journal.pgen.1003663

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Citations (207)

A nutrient-dependent division antagonist is regulated post-translationally by the Clp proteases inBacillus subtilis

bioRxiv (Cold Spring Harbor Laboratory) (2017)

Norbert S. Hill Jason D. Zuke Paul J. Buske An‐Chun Chien Petra Anne Levin

ABSTRACT Changes in nutrient availability have dramatic and well-defined impacts on both transcription and translation in bacterial cells. At the same time, the role of post-translational control in adaptation to nutrient-poor environments is poorly understood. Here we report a role for the bacterial Clp proteases in degradation of the division inhibitor UgtP during growth in nutrient-poor medium. Under nutrient-rich conditions, interactions with its substrate UDP-glucose promote interactions between UgtP and the tubulin-like cell division protein FtsZ in Bacillus subtilis , inhibiting maturation of the cytokinetic ring and increasing cell size. In nutrient-poor medium, reductions in UDP-glucose availability favor UgtP oligomerization, sequestering it from FtsZ and allowing division to occur at a smaller cell mass. Intriguingly, in nutrient-poor conditions UgtP levels are reduced ∼ 3-fold independent of UDP-glucose, suggesting an additional layer of regulation. B. subtilis cells cultured under different nutrient conditions indicate that UgtP accumulation is controlled through a nutrient-dependent post-translational mechanism dependent on the Clp proteases. Notably, all three B. subtilis Clp chaperones appeared able to target UgtP for degradation during growth in nutrient-poor conditions. Together these findings highlight conditional proteolysis as a mechanism for bacterial adaptation to a rapidly changing nutritional landscape.

FtsZ

Proteolysis

10.1101/176222

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Citations (0)

On a Robust, Sensitive Cell – Free Method for Pseudomonas Sensing and Quantification

bioRxiv (Cold Spring Harbor Laboratory) (2018)

Jong Seto Paul J. Buske Matthew T. Laurie

Cell – free lysates have found a utility in performing cellular functions and providing biologically-relevant metabolic products without the optimal biological conditions for growth and proliferation. By teasing out the biological components and constructing artificial conditions that enable for biological transcription and translation processes to occur, specific cell - like functions can be reconstituted in vitro without requiring the entire cell and milieu of cellular organelles. This enables for optimization of biological circuits, either by concentration or on/off switches, simply through the addition or removal of genetic components (plasmids, inducers, or repressors) of regulatory elements. Here, we demonstrate an application of cell – free process that is robust and portable, independent of a substrate, to apply for sensing and reporting functions of a quorum sensing molecule N-3-oxododecanoyl homoserine lactone (3OC12HSL) found crucial for pathological Pseudomonas infections. Using droplet microfluidics to integrate cell – free related functions into hydrogel scaffolds, we show that these cell - free circuits can be encapsulated, delivered, and activated in most environments—even in conditions with very little hydration.

Inducer

Cell Signaling

Cell-free system

Synthetic Biology

Organelle

10.1101/256438

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Citations (1)