The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus c cThe GenBank accession numbers for the sequences of clpPII-clpX and clpR-clpPIII reported in this paper are U92039 and AJ132005, respectively.

Schelin, Jenny; Lindmark, Fredrik; Clarke, Adrian K.

doi:10.1099/00221287-148-7-2255

Cited by 68 publications

(63 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…PCC 7942 to either low temperature or UV-B, but was not induced by heat shock Porankiewicz et al, 1998). Similarly, neither ClpP2, ClpP3 nor ClpP4 (ClpR) was shown to increase upon heat or cold shock (Schelin et al, 2002;Porankiewicz et al, 1998), whereas all four Clp proteins were induced by HL intensities to different degrees, but again the most pronounced increase was for ClpP1 in Synechococcus sp. PCC 7942 .…”

Section: Discussionmentioning

confidence: 87%

“…This is the case, for example, for the twocomponent system genes (Mary & Vaulot, 2003) or for the hsp genes examined in the present paper. Cyanobacteria have several hsp-like genes that encode chaperones and specific proteases (Schelin et al, 2002;Glatz et al, 1999). While the number of genes in the compact genome of Prochlorococcus is reduced for some gene categories (e.g.…”

Section: Discussionmentioning

confidence: 99%

“…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. PCC 7942 (Schelin et al, 2002). Similarly, while the DnaK2 protein of Synechococcus sp.…”

Section: Introductionmentioning

confidence: 99%

“…Stress-associated multigene family members appear to be differentially expressed under a variety of physiological conditions (Lindquist & Craig, 1988). 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).…”

Section: Introductionmentioning

confidence: 99%

“…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: 99%

See 4 more Smart Citations

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

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

View full text Add to dashboard Cite

show abstract

Consequences of the loss of catalytic triads in chloroplast CLPPR protease core complexes in vivo

et al. 2018

View full text Add to dashboard Cite

The essential chloroplast CLP protease system consists of a tetradecameric proteolytic core with catalytic P (P1, 3–6) and non‐catalytic R (R1–4) subunits, CLP chaperones and adaptors. The chloroplast CLP complex has a total of ten catalytic sites,but it is not known how many of these catalytic sites can be inactivated before plants lose viability. Here we show that CLPP3 and the catalytically inactive variant CLPP3S164A fully complement the developmental arrest of the clpp3‐1 null mutant, even under environmental stress. In contrast, whereas the inactive variant CLPP5S193A assembled into the CLP core, it cannot rescue the embryo lethal phenotype of the clpp5‐1 null mutant. This shows that CLPP3 makes a unique structural contribution but its catalytic site is dispensable, whereas the catalytic activity of CLPP5 is essential. Mass spectrometry of affinity‐purified CLP cores of the complemented lines showed highly enriched CLP cores. Other chloroplast proteins were co‐purified with the CLP cores and are candidate substrates. A strong overlap of co‐purified proteins between the CLP core complexes with active and inactive subunits indicates that CLP cores with reduced number of catalytic sites do not over‐accumulate substrates, suggesting that the bottle‐neck for degradation is likely substrate recognition and unfolding by CLP adaptors and chaperones, upstream of the CLP core.

show abstract

Functional Analysis of the Synechococcus elongatus PCC 7942 Genome

You

Holtman

Taton

et al. 2011

Advances in Photosynthesis and Respiration

View full text Add to dashboard Cite

The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus c cThe GenBank accession numbers for the sequences of clpPII-clpX and clpR-clpPIII reported in this paper are U92039 and AJ132005, respectively.

Cited by 68 publications

References 39 publications

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

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

Consequences of the loss of catalytic triads in chloroplast CLPPR protease core complexes in vivo

Functional Analysis of the Synechococcus elongatus PCC 7942 Genome

Contact Info

Product

Resources

About