The <i>Bacillus subtilis </i>DivIVA protein targets to the division septum and controls the site specificity of cell division

Edwards, David H.; Errington, Jeff

doi:10.1046/j.1365-2958.1997.3811764.x

Cited by 266 publications

(324 citation statements)

References 26 publications

(51 reference statements)

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“…Interestingly, one of these with similar domain organisation is DivIVA, another bacterial cytoskeletal protein that is essential for polarised growth in Actinomycetes (Flardh, 2003;Letek et al, 2008) whilst it controls cell division in others, such as Bacillus subtilis (Edwards et al, 2000;Edwards and Errington, 1997). It will be of great interest to establish to what extent Scy, FilP and DivIVA might share structural characteristics with potential relevance to their biological function.…”

Section: Discussionmentioning

confidence: 99%

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

Walshaw

Gillespie

Kelemen

2010

Journal of Structural Biology

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a b s t r a c tIn recent years, a number of bacterial coiled-coil proteins have been characterised which have roles in cell growth and morphology. Several have been shown to have a cytoskeletal function and some have been proposed to have an IF-like character in particular. We recently demonstrated in Streptomyces coelicolor a cytoskeletal role of Scy, a large protein implicated in filamentous growth, whose sequence is dominated by an unusual coiled-coil repeat. We present a detailed analysis of this 51-residue repeat and conclude that it is likely to form a parallel dimeric non-canonical coiled coil based on hendecads but with regions of local underwinding reflecting highly periodic modifications in the sequence. We also demonstrate that traditional sequence similarity searching is insufficient to identify all but the close orthologues of such repeat-dominated proteins, but that by an analysis of repeat periodicity and composition, remote homologues can be found. One clear candidate, despite a great size discrepancy and unremarkable sequence identity, is the known filament-former FilP in the same species. Both proteins appear distinct from the archetypal bacterial IF-like protein; they therefore may constitute a new class of bacterial filamentous protein. The similar sequence characteristics of both suggest their likely oligomer state and a possible mechanism for higher-order assembly into filaments. Another remote homologue in Actinomyces was highlighted by this method. Further, a known coiled-coil protein, DivIVA, appears to share some of these sequence characteristics.

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Section: Discussionmentioning

confidence: 99%

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

Walshaw

Gillespie

Kelemen

2010

Journal of Structural Biology

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“…Several lines of investigation provided insight into the genetic control of axial filament formation. The first was a study of the DivIVA protein of B. subtilis, considered the functional homologue of Escherichia coli MinE in that it restricts the division-inhibition proteins MinCD to the cell poles and so ensures mid-cell division during vegetative growth (34,56). divIVA mutants have severe growth and sporulation defects, but the isolation of mutants specifically defective in sporulation suggested that DivIVA played a dedicated role in development (Fig.…”

Section: Genetic Controlmentioning

confidence: 99%

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Hilbert

Piggot

2004

Microbiol Mol Biol Rev

318

432

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Gene expression in members of the family Bacillaceae becomes compartmentalized after the distinctive, asymmetrically located sporulation division. It involves complete compartmentalization of the activities of sporulation-specific sigma factors, σF in the prespore and then σE in the mother cell, and then later, following engulfment, σG in the prespore and then σK in the mother cell. The coupling of the activation of σF to septation and σG to engulfment is clear; the mechanisms are not. The σ factors provide the bare framework of compartment-specific gene expression. Within each σ regulon are several temporal classes of genes, and for key regulators, timing is critical. There are also complex intercompartmental regulatory signals. The determinants for σF regulation are assembled before septation, but activation follows septation. Reversal of the anti-σF activity of SpoIIAB is critical. Only the origin-proximal 30% of a chromosome is present in the prespore when first formed; it takes ≈15 min for the rest to be transferred. This transient genetic asymmetry is important for prespore-specific σF activation. Activation of σE requires σF activity and occurs by cleavage of a prosequence. It must occur rapidly to prevent the formation of a second septum. σG is formed only in the prespore. SpoIIAB can block σG activity, but SpoIIAB control does not explain why σG is activated only after engulfment. There is mother cell-specific excision of an insertion element in sigK and σE-directed transcription of sigK, which encodes pro-σK. Activation requires removal of the prosequence following a σG-directed signal from the prespore

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“…The result is that the mid-cell is left free for formation of the division plane. In the Gram-positive bacteria, including B. subtilis, a different topological specificity factor, DivIVA, achieves a similar result by recruiting the inhibitor to the cell poles and retaining it there (Cha & Stewart 1997;Edwards & Errington 1997;Marston et al 1998). In the presence of ATP, MinD binds to the division inhibitor MinC and goes to the membrane (Hu et al 1999Lackner et al 2003).…”

Section: A Common Mechanism Of Atp-dependent Dimerization and Atpase mentioning

confidence: 99%

Towards understanding the molecular basis of bacterial DNA segregation

Leonard

Møller‐Jensen

Löwe

2005

Phil. Trans. R. Soc. B

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Bacteria ensure the fidelity of genetic inheritance by the coordinated control of chromosome segregation and cell division. Here, we review the molecules and mechanisms that govern the correct subcellular positioning and rapid separation of newly replicated chromosomes and plasmids towards the cell poles and, significantly, the emergence of mitotic-like machineries capable of segregating plasmid DNA. We further describe surprising similarities between proteins involved in DNA partitioning (ParA/ParB) and control of cell division (MinD/MinE), suggesting a mechanism for intracellular positioning common to the two processes. Finally, we discuss the role that the bacterial cytoskeleton plays in DNA partitioning and the missing link between prokaryotes and eukaryotes that is bacterial mechano-chemical motor proteins.

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The Bacillus subtilis DivIVA protein targets to the division septum and controls the site specificity of cell division

Cited by 266 publications

References 26 publications

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

A novel coiled-coil repeat variant in a class of bacterial cytoskeletal proteins

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Towards understanding the molecular basis of bacterial DNA segregation

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