Poles Apart: Prokaryotic Polar Organelles and Their Spatial Regulation

Kirkpatrick, Clare L.; Viollier, Patrick H.

doi:10.1101/cshperspect.a006809

Cited by 32 publications

(27 citation statements)

References 99 publications

(159 reference statements)

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“…Examples include the chemotaxis complex in E. coli (49, 50) and in Caulobacter crescentus (51), the flagellum-dependent motility system in Vibrio , Pseudomonas , Helicobacter , and Campylobacter species, the flagellum-independent gliding motility in Myxococcus xanthus (52), and the control center of the PTS system in E. coli , which plays a central role in controlling the metabolic state in most bacterial cells depending on carbohydrate availability (15). Except for the PTS, all other polarly localized signaling systems have a membrane-anchored component(s).…”

Section: Discussionmentioning

confidence: 99%

The General Phosphotransferase System Proteins Localize to Sites of Strong Negative Curvature in Bacterial Cells

Govindarajan

Elisha

Nevo‐Dinur

et al. 2013

mBio

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The bacterial cell poles are emerging as subdomains where many cellular activities take place, but the mechanisms for polar localization are just beginning to unravel. The general phosphotransferase system (PTS) proteins, enzyme I (EI) and HPr, which control preferential use of carbon sources in bacteria, were recently shown to localize near the Escherichia coli cell poles. Here, we show that EI localization does not depend on known polar constituents, such as anionic lipids or the chemotaxis receptors, and on the cell division machinery, nor can it be explained by nucleoid occlusion or localized translation. Detection of the general PTS proteins at the budding sites of endocytotic-like membrane invaginations in spherical cells and their colocalization with the negative curvature sensor protein DivIVA suggest that geometric cues underlie localization of the PTS system. Notably, the kinetics of glucose uptake by spherical and rod-shaped E. coli cells are comparable, implying that negatively curved “pole-like” sites support not only the localization but also the proper functioning of the PTS system in cells with different shapes. Consistent with the curvature-mediated localization model, we observed the EI protein from Bacillus subtilis at strongly curved sites in both B. subtilis and E. coli. Taken together, we propose that changes in cell architecture correlate with dynamic survival strategies that localize central metabolic systems like the PTS to subcellular domains where they remain active, thus maintaining cell viability and metabolic alertness.

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Section: Discussionmentioning

confidence: 99%

The General Phosphotransferase System Proteins Localize to Sites of Strong Negative Curvature in Bacterial Cells

Govindarajan

Elisha

Nevo‐Dinur

et al. 2013

mBio

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“…Localization of polar proteins, which is the focus of this Commentary, is essential for a large number of important cellular processes in bacteria, including cell cycle regulation, cell differentiation, virulence, chemotaxis, motility and adhesion (Bowman et al, 2011;Kirkpatrick and Viollier, 2011). Our goal here is not to provide a survey of the large number of polar proteins described so far, many of which have been reviewed elsewhere (Ebersbach and Jacobs-Wagner, 2007;Dworkin, 2009;Kirkpatrick and Viollier, 2011;Davis and Waldor, 2013). Instead, our objective is to review and illustrate the general principles used by bacterial cells to localize proteins at the poles.…”

Section: Introductionmentioning

confidence: 99%

How do bacteria localize proteins to the cell pole?

Laloux

Jacobs‐Wagner

2014

Journal of Cell Science

163

158

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It is now well appreciated that bacterial cells are highly organized, which is far from the initial concept that they are merely bags of randomly distributed macromolecules and chemicals. Central to their spatial organization is the precise positioning of certain proteins in subcellular domains of the cell. In particular, the cell poles -the ends of rod-shaped cells -constitute important platforms for cellular regulation that underlie processes as essential as cell cycle progression, cellular differentiation, virulence, chemotaxis and growth of appendages. Thus, understanding how the polar localization of specific proteins is achieved and regulated is a crucial question in bacterial cell biology. Often, polarly localized proteins are recruited to the poles through their interaction with other proteins or protein complexes that were already located there, in a so-called diffusion-and-capture mechanism. Bacteria are also starting to reveal their secrets on how the initial pole 'recognition' can occur and how this event can be regulated to generate dynamic, reproducible patterns in time (for example, during the cell cycle) and space (for example, at a specific cell pole). Here, we review the major mechanisms that have been described in the literature, with an emphasis on the self-organizing principles. We also present regulation strategies adopted by bacterial cells to obtain complex spatiotemporal patterns of protein localization.

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“…Consequently, many proteins exhibit distinct patterns of subcellular localization, some of which arise due to active mechanisms (Shapiro et al 2009). For example, in rod-shaped bacteria, numerous proteins are localized to a cell pole, where they form complexes critical for processes such as chromosome segregation, motility, and chemotaxis (for review, see Gerdes et al 2010;Sourjik and Armitage 2010;Kirkpatrick and Viollier 2011). At least in some species, the sets of protein complexes found at the two cell poles (the old and new pole, respectively) differ, generating asymmetry between the two ends of the cell (Shapiro et al 2009).…”

mentioning

confidence: 99%

A family of ParA-like ATPases promotes cell pole maturation by facilitating polar localization of chemotaxis proteins

Ringgaard¹,

Schirner²,

Davis³

et al. 2011

Genes Dev.

105

162

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Stochastic processes are thought to mediate localization of membrane-associated chemotaxis signaling clusters in peritrichous bacteria. Here, we identified a new family of ParA-like ATPases (designated ParC ½for partitioning chemotaxis) encoded within chemotaxis operons of many polar-flagellated g-proteobacteria that actively promote polar localization of chemotaxis proteins. In Vibrio cholerae, a single ParC focus is found at the flagellated old pole in newborn cells, and later bipolar ParC foci develop as the cell matures. The cell cycle-dependent redistribution of ParC occurs by its release from the old pole and subsequent relocalization at the new pole, consistent with a ''diffusion and capture'' model for ParC dynamics. Chemotaxis proteins encoded in the same cluster as ParC have a similar unipolar-to-bipolar transition; however, they reach the new pole after the arrival of ParC. Cells lacking ParC exhibit aberrantly localized foci of chemotaxis proteins, reduced chemotaxis, and altered motility, which likely accounts for their enhanced colonization of the proximal small intestine in an animal model of cholera. Collectively, our findings indicate that ParC promotes the efficiency of chemotactic signaling processes. In particular, ParC-facilitated development of a functional chemotaxis apparatus at the new pole readies this site for its development into a functional old pole after cell division.

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Poles Apart: Prokaryotic Polar Organelles and Their Spatial Regulation

Cited by 32 publications

References 99 publications

The General Phosphotransferase System Proteins Localize to Sites of Strong Negative Curvature in Bacterial Cells

The General Phosphotransferase System Proteins Localize to Sites of Strong Negative Curvature in Bacterial Cells

How do bacteria localize proteins to the cell pole?

A family of ParA-like ATPases promotes cell pole maturation by facilitating polar localization of chemotaxis proteins

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