Oligomeric structure of the <i>Bacillus subtilis</i> cell division protein DivIVA determined by transmission electron microscopy

Stahlberg, Henning; Kutějová, Eva; Muchová, Katarı́na; Gregorini, Marco; Lustig, Ariel; Müller, Shirley A.; Olivieri, Vesna; Engel, Andréas; Wilkinson, Anthony J.; Barák, Imrich

doi:10.1111/j.1365-2958.2004.04074.x

Cited by 86 publications

(92 citation statements)

References 37 publications

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“…1B). Consistent with this notion, DivIVA oligomerizes in vitro and in vivo (Muchová et al, 2002;Stahlberg et al, 2004;Oliva et al, 2010), and these oligomers can further assemble into larger structures (Stahlberg et al, 2004;Wang et al, 2009). A 'molecular-bridging' model based on Monte-Carlo simulations argues that the clustering of DivIVA oligomers is favored at more-curved regions owing to the enhanced possibility of stabilizing interactions with the membrane (Lenarcic et al, 2009).…”

Section: Direct Sensing Of Enhanced Curvaturementioning

confidence: 55%

How do bacteria localize proteins to the cell pole?

Laloux

Jacobs‐Wagner

2014

Journal of Cell Science

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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Section: Direct Sensing Of Enhanced Curvaturementioning

confidence: 55%

How do bacteria localize proteins to the cell pole?

Laloux

Jacobs‐Wagner

2014

Journal of Cell Science

158

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“…On the other hand, polar localization did not allow us to exclude other functions, like chromosome segregation. The ability of DivIVA BS to oligomerize in vitro, forming elongated particles, the so-called "doggy-bone" structures, has been described previously (34,46). Moreover, DivIVA EF was recently found to self-interact in vivo (43).…”

Section: Discussionmentioning

confidence: 99%

“…An additional characteristic of DivIVA BS is its ability to form oligomers in vitro (34,46), and E. faecalis DivIVA (DivIVA EF ) can self-interact in vivo (43). Nothing is known about the interaction(s) of DivIVA with proteins other than itself.…”

mentioning

confidence: 99%

Streptococcus pneumoniaeDivIVA: Localization and Interactions in a MinCD-Free Context

et al. 2007

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To clarify the function of DivIVA in Streptococcus pneumoniae, we localized this protein in exponentially growing cells by both immunofluorescence microscopy and immunoelectron microscopy and found that S. pneumoniae DivIVA (DivIVA SPN ) had a unique localization profile: it was present simultaneously both as a ring at the division septum and as dots at the cell poles. Double-immunofluorescence analysis suggested that DivIVA is recruited to the septum at a later stage than FtsZ and is retained at the poles after cell separation. All the other cell division proteins that we tested were localized in the divIVA null mutant, although the percentage of cells having constricted Z rings was significantly reduced. In agreement with its localization profile and consistent with its coiled-coil nature, DivIVA interacted with itself and with a number of known or putative S. pneumoniae cell division proteins. Finally, a missense divIVA mutant, obtained by allelic replacement, allowed us to correlate, at the molecular level, the specific interactions and some of the facets of the divIVA mutant phenotype. Taken together, the results suggest that although the possibility of a direct role in chromosome segregation cannot be ruled out, DivIVA in S. pneumoniae seems to be primarily involved in the formation and maturation of the cell poles. The localization and the interaction properties of DivIVA SPN raise the intriguing possibility that a common, MinCD-independent function evolved differently in the various host backgrounds.A number of cell division proteins have been identified in Streptococcus pneumoniae and have been shown to localize at midcell to form the septal machinery (the septosome or divisome), consistent with what is known about the best-characterized rod-shaped model organisms, Escherichia coli and Bacillus subtilis (for recent reviews, see references 12, 16, 49, and 50).These proteins include the cell division initiator proteins FtsZ and FtsA, which are required at the early stages of the process (25,29,32), and some of the later proteins, DivIB/ FtsQ, DivIC/FtsB, FtsL, FtsW, PBP 2X, and PBP 1A (29,32,33,38), which are the septal markers for S. pneumoniae cells. Recent studies have confirmed that, overall, the major events in septation are conserved in S. pneumoniae. However, other aspects related to the division process, such as the associated morphological changes, the correct choice of the division site, and proper chromosome segregation, and the factors that regulate these aspects remain largely unknown.We have described characterization of a chromosome region in S. pneumoniae, downstream of the ftsZ gene, that is well conserved among gram-positive bacteria and is physically and transcriptionally related to the division and cell wall (dcw) cluster. We showed that functional inactivation of each of the five genes in the region resulted in defects in cell morphology, chromosome segregation, and/or cell division (13), and the importance of these genes in other species has been confirmed (18,23,30). In S. pneumonia...

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“…2C, bottom). Previous gel filtration analyses have indicated that purified DivIVA forms octamers and higher-order structures (18,30). Therefore, it seems plausible that the region beyond residue 130 indeed contains the tetramerization domain and that tetramerization is a prerequisite step for octamerization.…”

Section: C-terminal Diviva Truncations Interfere With Minj and Raca Bmentioning

confidence: 99%

Protein-Protein Interaction Domains of Bacillus subtilis DivIVA

Baarle

Celik

Kaval

et al. 2012

Journal of Bacteriology

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e DivIVA proteins are curvature-sensitive membrane binding proteins that recruit other proteins to the poles and the division septum. They consist of a conserved N-terminal lipid binding domain fused to a less conserved C-terminal domain. DivIVA homologues interact with different proteins involved in cell division, chromosome segregation, genetic competence, or cell wall synthesis. It is unknown how DivIVA interacts with these proteins, and we used the interaction of Bacillus subtilis DivIVA with MinJ and RacA to investigate this. MinJ is a transmembrane protein controlling division site selection, and the DNA-binding protein RacA is crucial for chromosome segregation during sporulation. Initial bacterial two-hybrid experiments revealed that the C terminus of DivIVA appears to be important for recruiting both proteins. However, the interpretation of these results is limited since it appeared that C-terminal truncations also interfere with DivIVA oligomerization. Therefore, a chimera approach was followed, making use of the fact that Listeria monocytogenes DivIVA shows normal polar localization but is not biologically active when expressed in B. subtilis. Complementation experiments with different chimeras of B. subtilis and L. monocytogenes DivIVA suggest that MinJ and RacA bind to separate DivIVA domains. Fluorescence microscopy of green fluorescent proteintagged RacA and MinJ corroborated this conclusion and suggests that MinJ recruitment operates via the N-terminal lipid binding domain, whereas RacA interacts with the C-terminal domain. We speculate that this difference is related to the cellular compartments in which MinJ and RacA are active: the cell membrane and the cytoplasm, respectively.

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Oligomeric structure of the Bacillus subtilis cell division protein DivIVA determined by transmission electron microscopy

Cited by 86 publications

References 37 publications

How do bacteria localize proteins to the cell pole?

How do bacteria localize proteins to the cell pole?

Streptococcus pneumoniaeDivIVA: Localization and Interactions in a MinCD-Free Context

Protein-Protein Interaction Domains of Bacillus subtilis DivIVA

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