Bacterial SOS Checkpoint Protein SulA Inhibits Polymerization of Purified FtsZ Cell Division Protein

Trusca, Dorina; Scott, S; Thompson, Chris; Bramhill, David

doi:10.1128/jb.180.15.3946-3953.1998

Cited by 162 publications

(104 citation statements)

References 41 publications

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“…With GDP, FtsZ assembles as curved ¢laments and minirings [25,27,28]. Helical tubules of FtsZ polymers were reported after polymerization with GDP or GTP in the presence of DEAE-dextran [27,34]. Similar tubes were found with FtsZ1 from M. jannaschii.…”

Section: Ftsz Polymer Morphologymentioning

confidence: 84%

“…Location in the FtsZ structure N43D [51] loop T2 (NBS) a D45A [36], D45N [51] loop T2 (NBS) A70T (ftsZ1) b [36,52] loop T3 (contacts GTP Q-phosphate) D86K [36] helix H3 G105S (ftsZ84) [9,44]v loop T4 (NBS) T108A (ftsZ3) [52] loop T4 (NBS) N165D, N165Y [51] loop T6 (NBS) M206C c loop T7 (AS) d N207C c , N207D [51] loop T7 (AS) D209A [36], D209C c , D209E c , D209N c loop T7 (AS) D212A [36], D212C [20], D212E [20], D212G (ftsZ2) [34,53], D212N [20] loop T7 (AS) D269A [36] loop between S8 and H10 e a NBS: Nucleotide-binding site: in direct contact with the nucleotide in the monomeric crystal structure [14]. b The original names of mutants, identi¢ed in screens for ftsZ mutants that were temperature-sensitive (ftsZ84) or resistant to cell division inhibitors (ftsZ1, ftsZ2 and ftsZ3), are given in brackets.…”

Section: Replacementmentioning

confidence: 99%

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The polymerization mechanism of the bacterial cell division protein FtsZ

Scheffers

Driessen

2001

FEBS Letters

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Bacteria and archaea usually divide symmetrically by formation of a septum in the middle of the cell. A key event in cell division is the assembly of the FtsZ ring. FtsZ is the prokaryotic homolog of tubulin and forms polymers in the presence of guanine nucleotides. Here, we specifically address the polymerization of FtsZ and the role of nucleotide hydrolysis in polymer formation and stabilization. Recent structural and biochemical results are discussed and a model for FtsZ polymerization, similar to that for tubulin, is presented. ß

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Section: Ftsz Polymer Morphologymentioning

confidence: 84%

Section: Replacementmentioning

confidence: 99%

The polymerization mechanism of the bacterial cell division protein FtsZ

Scheffers

Driessen

2001

FEBS Letters

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“…Lastly, the SOS response acts also on E. coli cell division by regulating several genes involved in septation. Most notably, induction of the sulA gene inhibits septum formation by interacting with the ftsZ gene product, leading to filamentation (Trusca et al, 1998), and the rationale for this process seems to lie in delaying cell division until DNA damage has been properly addressed. LexA is initially bound to its binding sites (SOS boxes) upstream of SOS genes, hindering their transcription by blocking RNA-polymerase activity.…”

Section: The E Coli Sos Responsementioning

confidence: 99%

Aeons of distress: an evolutionary perspective on the bacterial SOS response

2007

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The SOS response of bacteria is a global regulatory network targeted at addressing DNA damage. Governed by the products of the lexA and recA genes, it co-ordinates a comprehensive response against DNA lesions and its description in Escherichia coli has stood for years as a textbook paradigm of stress-response systems in bacteria. In this paper we review the current state of research on the SOS response outside E. coli. By retracing research on the identification of multiple diverging LexA-binding motifs across the Bacteria Domain, we show how this work has led to the description of a minimum regulon core, but also of a heterogeneous collection of SOS regulatory networks that challenges many tenets of the E. coli model. We also review recent attempts at reconstructing the evolutionary history of the SOS network that have cast new light on the SOS response. Exploiting the newly gained knowledge on LexA-binding motifs and the tight association of LexA with a recently described mutagenesis cassette, these works put forward likely evolutionary scenarios for the SOS response, and we discuss their relevance on the ultimate nature of this stress-response system and the evolutionary pressures driving its evolution.

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“…In addition, UVB-irradiated recA-expressing cells were elongated (Fig. 5b), an SOS regulon induced response to DNA damage mediated by the SulA cell division inhibitor protein (Trusca et al 1998). Confocal microscopy was utilized to visualise Pss TSG102/pTSG40 cells expressing gfp on bean leaf surfaces.…”

Section: Analysis Of Reca Expression In Pss Tsg102 On Bean Leaf Surfacesmentioning

confidence: 99%

Role of nucleotide excision repair and photoreactivation in the solar UVB radiation survival of Pseudomonas syringae pv. syringae B728a

Gunasekera

Sundin

2006

J Appl Microbiol

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Aims: To assess the role of DNA repair and photoreactivation in the solar radiation survival of the plant pathogen and leaf surface epiphyte Pseudomonas syringae pv. syringae (Pss). Methods and Results: Mutants of Pss B728a, with insertional mutations within the nucleotide excision repair gene uvrA, photolyase gene phr, or uvrA phr double mutants, were constructed to examine the importance of individual repair mechanisms in solar UV radiation (UVR) survival. The survival of either the uvrA mutant or the phr mutant was reduced by approx. 102‐fold following exposure to a dose of 4·5 kJ m−2 solar UVB (290–320 nm wavelengths) while the uvrA phr double mutant was reduced >106‐fold by the same dose. We constructed a transcriptional fusion between the Pss recA promoter and gfp to examine the induction of the SOS response in wild‐type and mutant strains. Initiation of the recA mediated SOS response was more rapid and peaked at higher levels in mutant strains suggesting both increased DNA damage in mutant strains and also that photoreactivation and nucleotide excision repair remove DNA damage as it is incurred which is reflected in a delay of recA expression. Visualization of expression of B728a cells containing the recA::gfp reporter on UVB‐irradiated bean leaves highlighted the movement of cells to intercellular spaces over time and that SOS induction was detectable when leaves were irradiated 48 h following leaf inoculation. Conclusions: This study indicated that solar UVB is detrimental to Pss B728a, DNA repair mechanisms play an important role in strain survival and expression of the SOS regulon on leaf surfaces contributes to survival of UVR‐exposed cells during plant colonization. Significance and Impact of the Study: This work links previous laboratory‐based UVR analyses with solar UVB dose‐response analyses and highlights the role of photoreactivation in delaying induction of the SOS response following solar irradiation. Knowledge of population dynamics following direct solar irradiation will enhance our understanding of the biology of Pss in the phyllosphere.

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Bacterial SOS Checkpoint Protein SulA Inhibits Polymerization of Purified FtsZ Cell Division Protein

Cited by 162 publications

References 41 publications

The polymerization mechanism of the bacterial cell division protein FtsZ

The polymerization mechanism of the bacterial cell division protein FtsZ

Aeons of distress: an evolutionary perspective on the bacterial SOS response

Role of nucleotide excision repair and photoreactivation in the solar UVB radiation survival of Pseudomonas syringae pv. syringae B728a

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