A model of membrane contraction predicting initiation and completion of bacterial cell division

Bacterial cell division involves a complex and dynamic sequence of events whereby polymers of the protein FtsZ assemble at the division plane and rearrange to achieve the goal of contracting the cell membrane at the site of cell division, thus dividing the parent cell into two daughter cells. We present a mathematical model (which we refer to as CAM-FF: Critical Accumulation of Membrane-bound FtsZ Fibres) of the assembly of the contractile ring in terms of the accumulation of short linear polymers of FtsZ that associate and dissociate from the cell membrane. In prokaryotes, the biochemical function of FtsZ is thought to underpin the assembly and at least the initial kinetic force of ring contraction. Our model extends earlier work of Surovtsev et al. [PLoS Comput. Biol., 2008, 4, e1000102] by adding (i) the kinetics of FtsZ accumulation on cell membrane anchor proteins and (ii) the physical forces required to deform the cell against its surface tension. Moreover, we provide a more rigorous treatment of intracellular diffusion and we revise some of the model parameter values in light of the experimental evidence now available. We derive a critical contraction parameter which links the chemical population dynamics of membrane-bound FtsZ molecules to the force of contraction. Using this parameter as a tool to predict the ability of the cell to initiate division, we are able to predict the division outcome in cells depleted of key FtsZ-binding proteins

Australian Sphingidae – DNA Barcodes Challenge Current Species Boundaries and Distributions

© 2014 Rougerie et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The attached file is the published version of the article

Global wildlife trade across the tree of life

Wildlife trade is a multibillion dollar industry that is driving species toward extinction. Of >31,500 terrestrial bird, mammal, amphibian, and squamate reptile species, ~18% (N = 5579) are traded globally. Trade is strongly phylogenetically conserved, and the hotspots of this trade are concentrated in the biologically diverse tropics. Using different assessment approaches, we predict that, owing to their phylogenetic replacement and trait similarity to currently traded species, future trade will affect up to 3196 additional species—totaling 8775 species at risk of extinction from trade. Our assessment underscores the need for a strategic plan to combat trade with policies that are proactive rather than reactive, which is especially important because species can quickly transition from being safe to being endangered as humans continue to harvest and trade across the tree of life

Staphylococcus aureus Survives with a Minimal Peptidoglycan Synthesis Machine but Sacrifices Virulence and Antibiotic Resistance

Many important cellular processes are performed by molecular machines, composed of multiple proteins that physically interact to execute biological functions. An example is the bacterial peptidoglycan (PG) synthesis machine, responsible for the synthesis of the main component of the cell wall and the target of many contemporary antibiotics. One approach for the identification of essential components of a cellular machine involves the determination of its minimal protein composition. Staphylococcus aureus is a Gram-positive pathogen, renowned for its resistance to many commonly used antibiotics and prevalence in hospitals. Its genome encodes a low number of proteins with PG synthesis activity (9 proteins), when compared to other model organisms, and is therefore a good model for the study of a minimal PG synthesis machine. We deleted seven of the nine genes encoding PG synthesis enzymes from the S. aureus genome without affecting normal growth or cell morphology, generating a strain capable of PG biosynthesis catalyzed only by two penicillin-binding proteins, PBP1 and the bi-functional PBP2. However, multiple PBPs are important in clinically relevant environments, as bacteria with a minimal PG synthesis machinery became highly susceptible to cell wall-targeting antibiotics, host lytic enzymes and displayed impaired virulence in a Drosophila infection model which is dependent on the presence of specific peptidoglycan receptor proteins, namely PGRP-SA. The fact that S. aureus can grow and divide with only two active PG synthesizing enzymes shows that most of these enzymes are redundant in vitro and identifies the minimal PG synthesis machinery of S. aureus. However a complex molecular machine is important in environments other than in vitro growth as the expendable PG synthesis enzymes play an important role in the pathogenicity and antibiotic resistance of S. aureus

Bringing traits back in the equation : A roadmap to understand species redistribution

Acknowledgments This research is a product of the BIOSHIFTS working group funded by the synthesis center (CESAB) of the French Foundation for Research on Biodiversity (FRB; www.fondationbiodiversite.fr) and the project FRAGSHIFTS funded by the Ministry of Ecological Transition (MTE), French Office for Biodiversity (OFB), and the French Foundation for Research on Biodiversity (FRB). We thank Holly Embke and two reviewers (including Tom Luhring) for their time and constructive comments that have improved the initial submission.Peer reviewe

Mechanisms, detection and impacts of species redistributions under climate change

International audienceShifts in species distributions are a common ecological response to climate change, and global temperature rise is often hypothesized as the primary driver. However, the directions and rates of distribution shifts are highly variable across species, systems, and studies, complicating efforts to manage and anticipate biodiversity responses to anthropogenic change. In this Review, we summarize approaches to documenting species range shifts, discuss why observed range shifts often do not match our expectations, and explore the impacts of species range shifts on nature and society. The majority (59%) of documented range shifts are directionally consistent with climate change, based on the BioShifts database of range shift observations. However, many observed species have not shifted or have shifted in directions opposite to temperature-based expectations. These lagging or expectation-contrary shifts might be explained by additional biotic or abiotic factors driving range shifts, including additional non-temperature climatic drivers, habitat characteristics, and species interactions, which are not normally considered in range shift documentations. Understanding and managing range shifts will require increasing and connecting observational biological data, generalizing range shift patterns across systems, and predicting shifts at management-relevant timescales

Kinetic Modeling of the Assembly, Dynamic Steady State, and Contraction of the FtsZ Ring in Prokaryotic Cytokinesis

Cytokinesis in prokaryotes involves the assembly of a polymeric ring composed of FtsZ protein monomeric units. The Z ring forms at the division plane and is attached to the membrane. After assembly, it maintains a stable yet dynamic steady state. Once induced, the ring contracts and the membrane constricts. In this work, we present a computational deterministic biochemical model exhibiting this behavior. The model is based on biochemical features of FtsZ known from in vitro studies, and it quantitatively reproduces relevant in vitro data. An essential part of the model is a consideration of interfacial reactions involving the cytosol volume, where monomeric FtsZ is dispersed, and the membrane surface in the cell's mid-zone where the ring is assembled. This approach allows the same chemical model to simulate either in vitro or in vivo conditions by adjusting only two geometrical parameters. The model includes minimal reactions, components, and assumptions, yet is able to reproduce sought-after in vivo behavior, including the rapid assembly of the ring via FtsZ-polymerization, the formation of a dynamic steady state in which GTP hydrolysis leads to the exchange of monomeric subunits between cytoplasm and the ring, and finally the induced contraction of the ring. The model gives a quantitative estimate for coupling between the rate of GTP hydrolysis and of FtsZ subunit turnover between the assembled ring and the cytoplasmic pool as observed. Membrane constriction is chemically driven by the strong tendency of GTP-bound FtsZ to self-assembly. The model suggests a possible mechanism of membrane contraction without a motor protein. The portion of the free energy of GTP hydrolysis released in cyclization is indirectly used in this energetically unfavorable process. The model provides a limit to the mechanistic complexity required to mimic ring behavior, and it highlights the importance of parallel in vitro and in vivo modeling