A role for division‐site‐selection protein MinD in regulation of internucleoid jumping of Soj (ParA) protein in <i>Bacillus subtilis</i>

Autret, Sabine; Errington, Jeff

doi:10.1046/j.1365-2958.2003.03264.x

Cited by 38 publications

(51 citation statements)

References 41 publications

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“…genes, perhaps partly because of loss of the putative interaction between Soj and MinD suggested previously (2). Overproduction of Soj resulted in elongated cells with less compact nucleoids, similar to the spo0J null mutant cells (Fig.…”

Section: Interaction Of Soj With Spo0j In Vivosupporting

confidence: 73%

Increasing the Ratio of Soj to Spo0J Promotes Replication Initiation inBacillus subtilis

et al. 2003

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The ParA and ParB protein families are well conserved in bacteria. However, their functions are still unclear. In Bacillus subtilis, Soj and Spo0J are members of these two protein families, respectively. A previous report revealed that replication initiated early and asynchronously in spo0J null mutant cells, as determined by flow cytometry. In this study, we examined the cause of this promotion of replication initiation. Deletion of both the soj and spo0J genes restored the frequency of replication initiation to almost the wild-type level, suggesting that production of Soj in the absence of Spo0J leads to early and asynchronous initiation of replication. Consistent with this suggestion, overproduction of Soj in wild-type cells had the same effect on replication initiation as in the spo0J null mutant, and overproduction of both Soj and Spo0J did not. These results indicate that when the ratio of Soj to Spo0J increases, Soj interferes with tight control of replication initiation and causes early and asynchronous initiation. Whereas replication initiation also occurred significantly earlier in the two spo0J mutants, spo0J14 and spo0J17, it occurred only slightly early in the sojK16Q mutant and was delayed in the sojG12V mutant. Although Soj localized to nucleoids in the spo0J mutants, the two Soj mutant proteins were distributed throughout the cell or localized to cell poles. Thus, interestingly, the promotion of replication initiation seems to correlate with localization of Soj to nucleoids. This may suggest that Soj inhibits transcription of some cell cycle genes and leads to early and asynchronous initiation of replication. In wild-type cells Spo0J counteracts this Soj function.The ParA and ParB protein families are widely conserved in bacteria and plasmids (47). These proteins were first analyzed in low-copy-number plasmids (including prophage) of Escherichia coli, such as F and P1, and were found to be essential for accurate partitioning of the plasmids (9, 17). The P1 ParA protein binds both ADP and ATP (7). The ATP-bound form interacts with the ParB-parS complex (parS:ParB-binding DNA sequence) and plays a direct role in partitioning (4). ParB stimulates a weak ATPase activity of ParA (8) and changes the ATP form to the ADP form that cannot interact with the ParB-parS complex. Thus, ParA-ADP is released from the ParB-parS complex and acts as repressor of the parAB operon by binding to the promoter region (4). The ParB protein was detected as foci within the cell, and its localization depended on ParA and parS (11), as expected from the biochemical data. Using a green fluorescent protein (GFP)-ParB fusion, Li and Austin (28) recently showed that P1 plasmid copies are suddenly separated into two daughter cells from the cell center immediately before cell division.In the case of the F plasmid, the biochemical activities of the ParA and ParB family members (SopA and SopB) are very similar to those of the P1 proteins (17). The cis-acting sopC region including the SopB-binding sequences was required for localizat...

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Section: Interaction Of Soj With Spo0j In Vivosupporting

confidence: 73%

Increasing the Ratio of Soj to Spo0J Promotes Replication Initiation inBacillus subtilis

et al. 2003

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“…Although it is tempting to speculate that Spo0J and Soj sense chromosome partitioning status and regulate the initiation of sporulation accordingly, direct evidence for this model is lacking. However, consistent with a role in monitoring the cell cycle, recent studies have linked these proteins to cell division, to initiation of DNA replication, and to axial filament formation (11,163,209,308).…”

Section: The Phosphorelaymentioning

confidence: 83%

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

Hilbert

Piggot

2004

Microbiol Mol Biol Rev

320

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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“…Thus, GFP-labeled Soj localizes in patches over nucleoid regions and undergoes irregular Spo0J-dependent internucleoid and intranucleoid movements (134,166), especially between nucleoids located near the two cell poles (9). Interestingly, the movements between nucleoids were partially dependent on the presence of MinD and also were suppressed by mutations that blocked cell division (9). The biological relevance of the dynamic behavior of Soj is unclear.…”

Section: The Mind/para Class Of Bacterial Cytoskeletal Proteinsmentioning

confidence: 99%

The Bacterial Cytoskeleton

Shih

Rothfield

2006

Microbiol Mol Biol Rev

243

220

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SUMMARY In recent years it has been shown that bacteria contain a number of cytoskeletal structures. The bacterial cytoplasmic elements include homologs of the three major types of eukaryotic cytoskeletal proteins (actin, tubulin, and intermediate filament proteins) and a fourth group, the MinD-ParA group, that appears to be unique to bacteria. The cytoskeletal structures play important roles in cell division, cell polarity, cell shape regulation, plasmid partition, and other functions. The proteins self-assemble into filamentous structures in vitro and form intracellular ordered structures in vivo. In addition, there are a number of filamentous bacterial elements that may turn out to be cytoskeletal in nature. This review attempts to summarize and integrate the in vivo and in vitro aspects of these systems and to evaluate the probable future directions of this active research field.

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A role for division‐site‐selection protein MinD in regulation of internucleoid jumping of Soj (ParA) protein in Bacillus subtilis

Cited by 38 publications

References 41 publications

Increasing the Ratio of Soj to Spo0J Promotes Replication Initiation inBacillus subtilis

Increasing the Ratio of Soj to Spo0J Promotes Replication Initiation inBacillus subtilis

Compartmentalization of Gene Expression duringBacillus subtilisSpore Formation

The Bacterial Cytoskeleton

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