Plastid chaperonin proteins Cpn60α and Cpn60β are required for plastid division in Arabidopsis thaliana

Suzuki, Kenji; Nakanishi, Hiromitsu; Bower, J.R. ed.; Yoder, David W.; Osteryoung, Katherine W.; Miyagishima, Shin-ya

doi:10.1186/1471-2229-9-38

Cited by 96 publications

(92 citation statements)

References 60 publications

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“…Analysis of the relative protein degradation changes with leaf growth rate (Figure 6) highlighted that while the degradation rate for the majority of the photosynthetic apparatus components positively correlated with growth ( Figure 6A), those of CPN60A and CPN60B negatively correlated with growth. These chaperonins are needed for plastid division (Suzuki et al, 2009), so their increased stabilization and abundance ( Figure 6F) are consistent with the more frequent chloroplast division events that occur in young leaves (Osteryoung and Pyke, 2014). The selective degradation changes observed in younger leaves could also be caused by specific changes in proteolysis and translational control when leaves are growing at a faster rate.…”

Section: Protein Abundance and Turnover Changes In Young Leaves With supporting

confidence: 48%

Protein Degradation Rate in Arabidopsis thaliana Leaf Growth and Development

et al. 2017

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We applied 15 N labeling approaches to leaves of the Arabidopsis thaliana rosette to characterize their protein degradation rate and understand its determinants. The progressive labeling of new peptides with 15 N and measuring the decrease in the abundance of >60,000 existing peptides over time allowed us to define the degradation rate of 1228 proteins in vivo. We show that Arabidopsis protein half-lives vary from several hours to several months based on the exponential constant of the decay rate for each protein. This rate was calculated from the relative isotope abundance of each peptide and the fold change in protein abundance during growth. Protein complex membership and specific protein domains were found to be strong predictors of degradation rate, while N-end amino acid, hydrophobicity, or aggregation propensity of proteins were not. We discovered rapidly degrading subunits in a variety of protein complexes in plastids and identified the set of plant proteins whose degradation rate changed in different leaves of the rosette and correlated with leaf growth rate. From this information, we have calculated the protein turnover energy costs in different leaves and their key determinants within the proteome.

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Section: Protein Abundance and Turnover Changes In Young Leaves With supporting

confidence: 48%

Protein Degradation Rate in Arabidopsis thaliana Leaf Growth and Development

et al. 2017

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“…By contrast, the DRP5B level increased, but the FtsZ2-1 (the antibodies are specific to FtsZ2-1 of three FtsZ proteins of Arabidopsis; Suzuki et al, 2009), and ARC6 levels remained constant during leaf development ( Figure 2B). Promoter-b-glucuronidase (GUS) fusion assays also showed that the activity of the PDV2 promoter is highest around the shoot apical meristem, in contrast with the FtsZ and DRP5B promoters ( Figure 2C).…”

Section: Resultsmentioning

confidence: 97%

The PLASTID DIVISION1 and 2 Components of the Chloroplast Division Machinery Determine the Rate of Chloroplast Division in Land Plant Cell Differentiation

et al. 2009

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In most algae, the chloroplast division rate is held constant to maintain the proper number of chloroplasts per cell. By contrast, land plants evolved cell and chloroplast differentiation systems in which the size and number of chloroplasts change along with their respective cellular function by regulation of the division rate. Here, we show that PLASTID DIVISION (PDV) proteins, land plant-specific components of the division apparatus, determine the rate of chloroplast division. Overexpression of PDV proteins in the angiosperm Arabidopsis thaliana and the moss Physcomitrella patens increased the number but decreased the size of chloroplasts; reduction of PDV levels resulted in the opposite effect. The level of PDV proteins, but not other division components, decreased during leaf development, during which the chloroplast division rate also decreased. Exogenous cytokinins or overexpression of the cytokinin-responsive transcription factor CYTOKININ RESPONSE FACTOR2 increased the chloroplast division rate, where PDV proteins, but not other components of the division apparatus, were upregulated. These results suggest that the integration of PDV proteins into the division machinery enabled land plant cells to change chloroplast size and number in accord with the fate of cell differentiation.

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“…Most wild-type chloroplasts contained only one Z-ring, though occasionally more were observed ( Figure 1C). By contrast, msl2 msl3 mutant chloroplasts frequently contained multiple Z-rings, some with a disorganized, forked appearance, similar to those observed in the arc11, arc3, mcd1, and parc6 mutants but distinct from those observed in other plastid division mutants, such as arc5, plastid division1 plastid division2 (pdv1 pdv2), or arc2 (Vitha et al, 2003;Miyagishima et al, 2006;Glynn et al, 2007Glynn et al, , 2009Fujiwara et al, 2008;Nakanishi et al, 2009a;Suzuki et al, 2009).…”

Section: Msl2 and Msl3 Are Required For Normal Z-ring Placementmentioning

confidence: 90%

“…Many established components of the plastid division apparatus were first identified as mutants with enlarged plastids, including nine arc mutants, cdp1, mcd1, pdv1, and br04 Leech, 1992, 1994;Miyagishima et al, 2006;Nakanishi et al, 2009a;Suzuki et al, 2009;Zhang et al, 2009). In this analysis of msl2 msl3 mutants, FtsZ ring formation was used as a cell-based marker for normal chloroplast division.…”

Section: Defective Chloroplast Division Explains the Enlarged Chloropmentioning

confidence: 99%

Two Mechanosensitive Channel Homologs Influence Division Ring Placement in Arabidopsis Chloroplasts

2011

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Chloroplasts must divide repeatedly to maintain their population during plant growth and development. A number of proteins required for chloroplast division have been identified, and the functional relationships between them are beginning to be elucidated. In both chloroplasts and bacteria, the future site of division is specified by placement of the Filamentous temperature sensitive Z (FtsZ) ring, and the Min system serves to restrict FtsZ ring formation to mid-chloroplast or mid-cell. How the Min system is regulated in response to environmental and developmental factors is largely unstudied. Here, we investigated the role in chloroplast division played by two Arabidopsis thaliana homologs of the bacterial mechanosensitive (MS) channel MscS: MscS-Like 2 (MSL2) and MSL3. Immunofluorescence microscopy and live imaging approaches demonstrated that msl2 msl3 double mutants have enlarged chloroplasts containing multiple FtsZ rings. Genetic analyses indicate that MSL2, MSL3, and components of the Min system function in the same pathway to regulate chloroplast size and FtsZ ring formation. In addition, an Escherichia coli strain lacking MS channels also showed aberrant FtsZ ring assembly. These results establish MS channels as components of the chloroplast division machinery and suggest that their role is evolutionarily conserved.

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Plastid chaperonin proteins Cpn60α and Cpn60β are required for plastid division in Arabidopsis thaliana

Cited by 96 publications

References 60 publications

Protein Degradation Rate in Arabidopsis thaliana Leaf Growth and Development

Protein Degradation Rate in Arabidopsis thaliana Leaf Growth and Development

The PLASTID DIVISION1 and 2 Components of the Chloroplast Division Machinery Determine the Rate of Chloroplast Division in Land Plant Cell Differentiation

Two Mechanosensitive Channel Homologs Influence Division Ring Placement in Arabidopsis Chloroplasts

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