DivIVA Is Required for Polar Growth in the MreB-Lacking Rod-Shaped Actinomycete<i>Corynebacterium glutamicum</i>

Letek, Michal; Ordóñez, Efrén; Vaquera, José; Margolin, William; Flärdh, Klas; Mateos, Luís M.; Gil, José A.

doi:10.1128/jb.01934-07

Cited by 130 publications

(149 citation statements)

References 47 publications

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“…Although these modes of cell growth are generally thought to be predominant among rod-shaped bacteria, in Actinobacteria, elongation occurs at the cell poles and requires the polarity determinant protein DivIVA (3)(4)(5)(6)(7)(8). In addition, a striking type of polar growth is found within some Alphaproteobacteria that grow by budding (9) (Fig.…”

mentioning

confidence: 99%

Polar growth in the Alphaproteobacterial order Rhizobiales

Brown

Pedro

Kysela

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

202

254

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Elongation of many rod-shaped bacteria occurs by peptidoglycan synthesis at discrete foci along the sidewall of the cells. However, within the Rhizobiales, there are many budding bacteria, in which new cell growth is constrained to a specific region. The phylogeny of the Rhizobiales indicates that this mode of zonal growth may be ancestral. We demonstrate that the rod-shaped bacterium Agrobacterium tumefaciens grows unidirectionally from the new pole generated after cell division and has an atypical peptidoglycan composition. Polar growth occurs under all conditions tested, including when cells are attached to a plant root and under conditions that induce virulence. Finally, we show that polar growth also occurs in the closely related bacteria Sinorhizobium meliloti , Brucella abortus , and Ochrobactrum anthropi . We find that unipolar growth is an ancestral and conserved trait among the Rhizobiales, which includes important mutualists and pathogens of plants and animals.

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mentioning

confidence: 99%

Polar growth in the Alphaproteobacterial order Rhizobiales

Brown

Pedro

Kysela

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

202

254

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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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“…No concomitant degradation or decrease in cellular DivIVA content is observed, suggesting that high AfsK activity causes disassembly of the DivIVA-containing apical polarisome. DivIVA is a self-assembling coiled-coil protein that forms oligomers and higher-order complexes and is involved in polar targeting in a range of Gram-positive bacteria (15,30,(38)(39)(40). The AfsK-mediated phosphorylation of DivIVA in Streptomyces occurs on two trypsin-generated fragments in the C-terminal domain (Fig.…”

Section: Discussionmentioning

confidence: 99%

The Ser/Thr protein kinase AfsK regulates polar growth and hyphal branching in the filamentous bacteria Streptomyces

Hempel

Cantlay

Molle

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

108

155

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In cells that exhibit apical growth, mechanisms that regulate cell polarity are crucial for determination of cellular shape and for the adaptation of growth to intrinsic and extrinsic cues. Broadly conserved pathways control cell polarity in eukaryotes, but less is known about polarly growing prokaryotes. An evolutionarily ancient form of apical growth is found in the filamentous bacteria Streptomyces, and is directed by a polarisome-like complex involving the essential protein DivIVA. We report here that this bacterial polarization machinery is regulated by a eukaryotic-type Ser/Thr protein kinase, AfsK, which localizes to hyphal tips and phosphorylates DivIVA. During normal growth, AfsK regulates hyphal branching by modulating branch-site selection and some aspect of the underlying polarisome-splitting mechanism that controls branching of Streptomyces hyphae. Further, AfsK is activated by signals generated by the arrest of cell wall synthesis and directly communicates this to the polarisome by hyperphosphorylating DivIVA. Induction of high levels of DivIVA phosphorylation by using a constitutively active mutant AfsK causes disassembly of apical polarisomes, followed by establishment of multiple hyphal branches elsewhere in the cell, revealing a profound impact of this kinase on growth polarity. The function of AfsK is reminiscent of the phoshorylation of polarity proteins and polarisome components by Ser/Thr protein kinases in eukaryotes.hyphal growth | protein phosphorylation | peptidoglycan | cytoskeleton | tip extension

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DivIVA Is Required for Polar Growth in the MreB-Lacking Rod-Shaped ActinomyceteCorynebacterium glutamicum

Cited by 130 publications

References 47 publications

Polar growth in the Alphaproteobacterial order Rhizobiales

Polar growth in the Alphaproteobacterial order Rhizobiales

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

The Ser/Thr protein kinase AfsK regulates polar growth and hyphal branching in the filamentous bacteria Streptomyces

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