Cell cycle‐dependent abundance, stability and localization of FtsA and FtsQ in <i>Caulobacter crescentus</i>

Martín, Miriam; Trimble, Michael J.; Brun, Yves V.

doi:10.1111/j.1365-2958.2004.04251.x

Cited by 46 publications

(64 citation statements)

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“…For example, there is more co-dependency of recruitment in B. subtilis 92 . In contrast to B. subtilis and E. coli, C. crescentus cell-division proteins are specifically synthesized and degraded during the cell cycle in parallel with their requirement: FtsA and FtsQ, which function after FtsZ, are synthesized and stable in predivisional cells, but are degraded post-division when they are no longer needed 93 . The septation process in round-shaped bacteria such as streptococci and staphylococci involves many of the same proteins, but their growth is normally dependent on the septation machinery 94 .…”

Section: Ftsz Function In Bacteria Assembly Of the Cytokinesis Machinementioning

confidence: 99%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

560

484

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Binary fission of many prokaryotes as well as some eukaryotic organelles depends on the FtsZ protein, which self-assembles into a membrane-associated ring structure early in the division process. FtsZ is homologous to tubulin, the building block of the microtubule cytoskeleton in eukaryotes. Recent advances in genomics and cell-imaging techniques have paved the way for the remarkable progress in our understanding of fission in bacteria and organelles.Duplication of cells occurs by the division of a mother cell into two daughter cells. This process, known as cytokinesis, provides the force to split cells and is spatially regulated to faithfully partition the genetic material. The cytoskeleton has a crucial role in cytokinesis. In animal and fungal cells, a medial ring of actin and myosin, helped by other proteins, contracts to divide the cell. Plant cells use a cell plate, and are guided by actin filaments and microtubules. Prokaryotes, which include bacteria and archaea, possess homologues of eukaryotic cytoskeletal proteins. Most prokaryotes use a tubulin homologue, a protein known as FtsZ, to divide. Eukaryotic organelles such as chloroplasts and mitochondria evolved from bacteria, and all chloroplasts and some mitochondria use FtsZ to divide.FtsZ is thought to be the first protein to localize to the site of future division in bacteria 1 , and it assembles into what is known as the Z ring (FIG. 1). In Escherichia coli, the Z ring recruits at least ten other proteins, all of which are required for the progression and completion of cytokinesis 2 , as will be discussed below. Whereas the cytokinetic apparatus in eukaryotic cells and even organelles can be observed directly in stained thin sections by transmission electron microscopy, the Z ring and its associated factors are not detectable by these methods. This is probably because the protein machinery is largely membrane bound and resides in a densely populated cytoplasmic environment. However, the development of green fluorescent protein (GFP) fusion and improved immunofluorescence techniques over the past 10 years have been crucial in allowing the first direct visualization of many cellular components and their dynamics. For example, using GFP fusions, the dynamics of the Z ring and other components of the cell-division protein machinery can now be visualized in living bacterial cells. The combination of these new cytological tools with genomics and the Competing interests statementThe author declares no competing financial interests. HHS Public Access Author Manuscript Author ManuscriptAuthor ManuscriptAuthor Manuscript already powerful genetics of several model systems have spurred rapid progress in our understanding of the molecular cell biology of bacteria and eukaryotic organelles. This review will discuss how the recent revolutions in genomics and cell biology have provided new evolutionary and mechanistic insights into how bacterial cells and organelles divide. The FtsZ family of proteins Conservation of FtsZFtsZ is a highly conserved protein ...

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Section: Ftsz Function In Bacteria Assembly Of the Cytokinesis Machinementioning

confidence: 99%

FtsZ and the division of prokaryotic cells and organelles

Margolin

2005

Nat Rev Mol Cell Biol

560

484

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“…Thus, transcriptional regulation alone is unlikely to temporally regulate Z-ring assembly. This may be different for C. crescentus, where FtsA and FtsQ have been shown to be specifically synthesized when required for assembly and then rapidly degraded when no longer needed (266). There are several negative regulatory systems described thus far ( Table 4) that ensure that Z-ring assembly is neither at the poles, where unequal partitioning of DNA would occur, or on top of nucleoids, where chromosomes would be decapitated (340,341).…”

Section: What Are the Negative Regulators Of Ftsz Assembly?mentioning

confidence: 99%

Bacterial Growth and Cell Division: a Mycobacterial Perspective

Hett

Rubín

2008

Microbiol Mol Biol Rev

342

293

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SUMMARY The genus Mycobacterium is best known for its two major pathogenic species, M. tuberculosis and M. leprae, the causative agents of two of the world's oldest diseases, tuberculosis and leprosy, respectively. M. tuberculosis kills approximately two million people each year and is thought to latently infect one-third of the world's population. One of the most remarkable features of the nonsporulating M. tuberculosis is its ability to remain dormant within an individual for decades before reactivating into active tuberculosis. Thus, control of cell division is a critical part of the disease. The mycobacterial cell wall has unique characteristics and is impermeable to a number of compounds, a feature in part responsible for inherent resistance to numerous drugs. The complexity of the cell wall represents a challenge to the organism, requiring specialized mechanisms to allow cell division to occur. Besides these mycobacterial specializations, all bacteria face some common challenges when they divide. First, they must maintain their normal architecture during and after cell division. In the case of mycobacteria, that means synthesizing the many layers of complex cell wall and maintaining their rod shape. Second, they need to coordinate synthesis and breakdown of cell wall components to maintain integrity throughout division. Finally, they need to regulate cell division in response to environmental stimuli. Here we discuss these challenges and the mechanisms that mycobacteria employ to meet them. Because these organisms are difficult to study, in many cases we extrapolate from information known for gram-negative bacteria or more closely related GC-rich gram-positive organisms.

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“…For example, during the G1 to S transition, ClpXP localizes at the cell pole where it is responsible for the proteolysis of several polarly-localized proteins including flagellar components and CtrA, a master regulator in C. crescentus that prevents DNA replication (22)(23)(24). After DNA replication, ClpXP reaches the cell division ring, in order to clear divisome components from the daughter swarmer cell (33,34). How ClpXP recognizes CcTrx1 as a substrate in predivisional cells is unclear.…”

Section: Discussionmentioning

confidence: 99%

An essential thioredoxin is involved in the control of the cell cycle in the bacterium Caulobacter crescentus

Goemans

Beaufay

Wahni

et al. 2018

Journal of Biological Chemistry

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Thioredoxins (Trxs) are antioxidant proteins that are conserved among all species. These proteins have been extensively studied and perform reducing reactions on a broad range of substrates. Here, we identified Caulobacter crescentus Trx1 (CCNA_03653; CcTrx1) as an oxidoreductase that is involved in the cell cycle progression of this model bacterium and is required to sustain life. Intriguingly, the abundance of CcTrx1 varies throughout the C. crescentus cell cycle: while the expression of CcTrx1 is induced in stalked cells, right before DNA replication initiation, CcTrx1 is actively degraded by the ClpXP protease in predivisional cells. Importantly, we demonstrated that regulation of the abundance of CcTrx1 is crucial for cell growth and survival as modulating CcTrx1 levels leads to cell death. Finally, we also report a comprehensive biochemical and structural characterization of this unique and essential Trx. The requirement to precisely control the abundance of CcTrx1 for cell survival underlines the importance of redox control for optimal cell cycle progression in C. crescentus. INTRODUCTIONThioredoxins (Trx) are small antioxidant proteins that have been identified in most living organisms. They receive electrons from NADPH through the flavoprotein thioredoxin reductase and catalyze the reduction of oxidized cysteine residues in substrate proteins (1). As such, they are implicated in a variety of processes, ranging from oxidative stress defense to signal transduction. These soluble proteins all share a similar structure, a Trx-fold consisting of five b-strands surrounded by 4 ahelices. They also display a strictly conserved WCGPC catalytic active site motif and contain a cis-proline residue (1). The two cysteines of the catalytic motif are the key players involved in the reduction of oxidized substrates.First identified in 1964 as an electron donor for ribonucleotide reductase (2,3), Escherichia coli Trx1 (EcTrx1) is a major http://www.jbc.org/cgi

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Cell cycle‐dependent abundance, stability and localization of FtsA and FtsQ in Caulobacter crescentus

Abstract: SummaryCoordination between cell division and DNA replication is ensured by checkpoints that act through proteins required for cell division. Following a block in DNA replication, transcription of the cell division progression genes ftsA and ftsQ is prevented in

Cited by 46 publications

References 64 publications

FtsZ and the division of prokaryotic cells and organelles

FtsZ and the division of prokaryotic cells and organelles

Bacterial Growth and Cell Division: a Mycobacterial Perspective

An essential thioredoxin is involved in the control of the cell cycle in the bacterium Caulobacter crescentus

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