Essential role of DivIVA in polar growth and morphogenesis in <i>Streptomyces coelicolor</i> A3(2)

Flärdh, Klas

doi:10.1046/j.1365-2958.2003.03660.x

Cited by 206 publications

(260 citation statements)

References 52 publications

(70 reference statements)

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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.

199

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.

199

254

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“…Inactivation of this gene in B. subtilis results in mini-cells, and its overexpression causes a filamentous phenotype. In S. coelicolor, DivIVA SC is essential and is localized to the growing tips and lateral branches of hyphae where new peptidoglycan assembly occurs (Flardh 2003). Overexpression of this gene causes hyperbranching, with broad cells and abnormal tip growth, a phenotype similar to that of the pknA-overexpressing mycobacterial cells.…”

Section: Discussionmentioning

confidence: 99%

“…This phosphorylation site is consistent with the preferred motif identified by peptide library screening and is remarkably similar to the phosphorylation site of Rv1422 (AT*QEIP) (see Supplementary Figs. 3, 4 for mass spectra of both phosphopeptides). Wag31 was originally identified as an antigen of M. tuberculosis, but comparative sequence analysis indicates that it is a homolog of the cell division/cell shape protein DivIVA of gram-positive bacteria (Hermans et al 1995;Flardh 2003). We were unable to identify discrete protein spots in the protein gels corresponding to spots IV and V on the immunoblots, so mass spectrometry analysis was not performed for these spots.…”

Section: Identification Of In Vivo Substrates Of Pkna and Pknbmentioning

confidence: 99%

The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape

Kang¹,

Abbott²,

Park³

et al. 2005

Genes Dev.

356

470

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The Mycobacterium tuberculosis genome contains 11 serine/threonine kinase genes including two, pknA and pknB, that are part of an operon encoding genes involved in cell shape control and cell wall synthesis. Here we demonstrate that pknA and pknB are predominantly expressed during exponential growth, and that overexpression of these kinases slows growth and alters cell morphology. We determined the preferred substrate motifs of PknA and PknB, and identified three in vivo substrates of these kinases: PknB; Wag31, an ortholog of the cell division protein DivIVA; and Rv1422, a conserved protein of unknown function. Expression of different alleles of wag31 in vivo alters cell shape, in a manner dependent on the phosphoacceptor residue in the protein produced. Partial depletion of pknA or pknB results in narrow, elongated cells. These data indicate that signal transduction mediated by these kinases is a novel mechanism for the regulation of cell shape in mycobacteria, one that may be conserved among gram-positive bacteria.[Keywords: Kinase; DivIVA; peptide library screen; mycobacteria] Supplemental material is available at http://www.genesdev.org.

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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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Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2)

Cited by 206 publications

References 52 publications

Polar growth in the Alphaproteobacterial order Rhizobiales

Polar growth in the Alphaproteobacterial order Rhizobiales

The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape

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

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