Multiple clpP Genes for the Proteolytic Subunit of the Atp-Dependent Clp Protease in the Cyanobacterium Synechococcus sp. PCC 7942

Clarke, Adrian K.; Schelin, Jenny; Porankiewicz, Joanna

doi:10.1007/978-1-4615-4827-0_85

Cited by 8 publications

(14 citation statements)

References 12 publications

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“…strain PCC7942 led to altered bacterial division, with the cells remaining attached after septum formation. On the other hand, the inactivation of cyanobacterial clpP1 caused the formation of severely elongated cells, a morphological phenotype previously reported for the B. subtilis clpP mutant (6,43).…”

Section: Discussionsupporting

confidence: 56%

DistinctclpPGenes Control Specific Adaptive Responses inBacillus thuringiensis

et al. 2002

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ClpP and ClpC are subunits of the Clp ATP-dependent protease, which is ubiquitous among prokaryotic and eukaryotic organisms. The role of these proteins in stress tolerance, stationary-phase adaptive responses, and virulence in many bacterial species has been demonstrated. Based on the amino acid sequences of the Bacillus subtilis clpC and clpP genes, we identified one clpC gene and two clpP genes (designated clpP1 and clpP2) in Bacillus thuringiensis. Predicted proteins ClpP1 and ClpP2 have approximately 88 and 67% amino acid sequence identity with ClpP of B. subtilis, respectively. Inactivation of clpC in B. thuringiensis impaired sporulation efficiency. The clpP1 and clpP2 mutants were both slightly susceptible to salt stress, whereas disruption of clpP2 negatively affected sporulation and abolished motility. Virulence of the clp mutants was assessed by injecting bacteria into the hemocoel of Bombyx mori larvae. The clpP1 mutant displayed attenuated virulence, which appeared to be related to its inability to grow at low temperature (25°C), suggesting an essential role for ClpP1 in tolerance of low temperature. Microscopic examination of clpP1 mutant cells grown at 25°C showed altered bacterial division, with cells remaining attached after septum formation. Analysis of lacZ transcriptional fusions showed that clpP1 was expressed at 25 and 37°C during the entire growth cycle. In contrast, clpP2 was expressed at 37°C but not at 25°C, suggesting that ClpP2 cannot compensate for the absence of ClpP1 in the clpP1 mutant cells at low temperature. Our study demonstrates that ClpP1 and ClpP2 control distinct cellular regulatory pathways in B. thuringiensis.

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Section: Discussionsupporting

confidence: 56%

DistinctclpPGenes Control Specific Adaptive Responses inBacillus thuringiensis

et al. 2002

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“…strain PCC 7942 has genes encoding three ClpP isoenzymes and a single copy of ClpX. Viable deletion-insertion mutants of Synechococcus were obtained only for clpPI and clpPII, suggesting that clpPIII and clpX are indispensable for growth (6,23). ClpX and ClpP are both essential in C. crescentus (7,15), and chaperone functions have been ascribed to ClpX besides its role in ClpXP proteolysis (17,24,30).…”

Section: Vol 185 2003 Notes 2963mentioning

confidence: 99%

Essentiality of clpX , but Not clpP , clpL , clpC , or clpE , in Streptococcus pneumoniae R6

Robertson

Gilmour

et al. 2003

J Bacteriol

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We show by using a regulated promoter that clpX of Streptococcus pneumoniae R6 is essential, whereas clpP, clpL, clpC, and clpE can be disrupted. The essentiality of clpX was initially missed because of duplication and rearrangement in the region of the chromosome containing clpX. Depletion of ClpX resulted in a rapid loss of viability without overt changes in cell morphology. Essentiality of clpX, but not clpP, has not been reported previously

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“…As an example, cyanobacteria possess four clpP genes (Porankiewicz et al, 1999;Schelin et al, 2002). clpP1 is monocistronic, while clpP2 and clpP3, similar to the situation in Escherichia coli, appear to be arranged in an operon with clpX (Schelin et al, 2002;Clarke et al, 1998) and clpP4 (also called clpR, encoding a protein that lacks the three active-site amino acids representative of ClpP proteases), respectively (Schelin et al, 2002). Unlike most bacterial Clp proteins, and especially ClpP1 , the ClpP2, ClpP3, ClpP4 and ClpX polypeptides did not accumulate to high levels upon cold shock, oxidative stress or HL exposure of Synechococcus sp.…”

Section: Introductionmentioning

confidence: 95%

Effects of high light on transcripts of stress-associated genes for the cyanobacteria Synechocystis sp. PCC 6803 and Prochlorococcus MED4 and MIT9313

Mary

Grossman

et al. 2004

Microbiology

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Cyanobacteria constitute an ancient, diverse and ecologically important bacterial group. The responses of these organisms to light and nutrient conditions are finely controlled, enabling the cells to survive a range of environmental conditions. In particular, it is important to understand how cyanobacteria acclimate to the absorption of excess excitation energy and how stress-associated transcripts accumulate following transfer of cells from low-to high-intensity light. In this study, quantitative RT-PCR was used to monitor changes in levels of transcripts encoding chaperones and stress-associated proteases in three cyanobacterial strains that inhabit different ecological niches: the freshwater strain Synechocystis sp. PCC 6803, the marine high-light-adapted strain Prochlorococcus MED4 and the marine low-light-adapted strain Prochlorococcus MIT9313. Levels of transcripts encoding stress-associated proteins were very sensitive to changes in light intensity in all of these organisms, although there were significant differences in the degree and kinetics of transcript accumulation. A specific set of genes that seemed to be associated with high-light adaptation (groEL/groES, dnaK2, dnaJ3, clpB1 and clpP1) could be targeted for more detailed studies in the future. Furthermore, the strongest responses were observed in Prochlorococcus MED4, a strain characteristic of the open ocean surface layer, where hsp genes could play a critical role in cell survival.

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Multiple clpP Genes for the Proteolytic Subunit of the Atp-Dependent Clp Protease in the Cyanobacterium Synechococcus sp. PCC 7942

Cited by 8 publications

References 12 publications

DistinctclpPGenes Control Specific Adaptive Responses inBacillus thuringiensis

DistinctclpPGenes Control Specific Adaptive Responses inBacillus thuringiensis

Essentiality of clpX , but Not clpP , clpL , clpC , or clpE , in Streptococcus pneumoniae R6

Effects of high light on transcripts of stress-associated genes for the cyanobacteria Synechocystis sp. PCC 6803 and Prochlorococcus MED4 and MIT9313

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