Photodamaged D1 protein is degraded in <i>Arabidopsis</i> mutants lacking the Deg2 protease

Huesgen, Pitter F.; Schuhmann, Holger; Adamska, Iwona

doi:10.1016/j.febslet.2006.11.058

Cited by 57 publications

(51 citation statements)

References 32 publications

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“…We examined several available Arabidopsis mutant lines deficient in the chloroplast proteases FtsH2, FtsH5 (Kato et al, 2009), Deg2 (Huesgen et al, 2006), Deg5, Deg8 (Sun et al, 2007), and ClpR1 (Stanne et al, 2009) after a shift from blue light to far-red light. Some of these proteases act on the stromal side of the thylakoid membrane while others act on the lumen side or in the stroma.…”

Section: Resultsmentioning

confidence: 99%

The Phosphorylation Status of the Chloroplast Protein Kinase STN7 of Arabidopsis Affects Its Turnover

et al. 2011

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The chloroplast serine-threonine protein kinase STN7 of Arabidopsis (Arabidopsis thaliana) is required for the phosphorylation of the light-harvesting system of photosystem II and for state transitions, a process that allows the photosynthetic machinery to balance the light excitation energy between photosystem II and photosystem I and thereby to optimize the photosynthetic yield. Because the STN7 protein kinase of Arabidopsis is known to be phosphorylated at four serine-threonine residues, we have changed these residues by site-directed mutagenesis to alanine (STN7-4A) or aspartic acid (STN7-4D) to assess the role of these phosphorylation events. The corresponding mutants were still able to phosphorylate the light-harvesting system of photosystem II and to perform state transitions. Moreover, we noticed a marked decrease in the level of the STN7 kinase in the wild-type strain under prolonged state 1 conditions that no longer occurs in the STN7-4D mutant. The results suggest a possible role of phosphorylation of the STN7 kinase in regulating its turnover.

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Section: Resultsmentioning

confidence: 99%

The Phosphorylation Status of the Chloroplast Protein Kinase STN7 of Arabidopsis Affects Its Turnover

et al. 2011

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“…In an in vitro study, recombinant Deg2 was demonstrated to cleave the D1 protein of photosystem II (PSII) after exposure to high light intensity (Haussuhl et al, 2001). However, a recent in vivo study with mutants lacking Deg2 demonstrated that their rate of D1 degradation under light stress conditions was comparable to that of wild-type plants, suggesting that Deg2 is not essential for D1 degradation (Huesgen et al, 2006). No other in vivo studies of the function of plant Deg proteases have been reported to date.…”

Section: Introductionmentioning

confidence: 97%

The Thylakoid Lumen Protease Deg1 Is Involved in the Repair of Photosystem II from Photoinhibition in Arabidopsis

2007

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Deg1 is a Ser protease peripherally attached to the lumenal side of the thylakoid membrane. Its physiological function is unknown, but its localization makes it a suitable candidate for participation in photoinhibition repair by degradation of the photosystem II reaction center protein D1. We transformed Arabidopsis thaliana with an RNA interference construct and obtained plants with reduced levels of Deg1. These plants were smaller than wild-type plants, flowered earlier, were more sensitive to photoinhibition, and accumulated more of the D1 protein, probably in an inactive form. Two C-terminal degradation products of the D1 protein, of 16 and 5.2 kD, accumulated at lower levels compared with the wild type. Moreover, addition of recombinant Deg1 to inside-out thylakoid membranes isolated from the mutant could induce the formation of the 5.2-kD D1 C-terminal fragment, whereas the unrelated proteases trypsin and thermolysin could not. Immunoblot analysis revealed that mutants containing less Deg1 also contain less FtsH protease, and FtsH mutants contain less Deg1. These results suggest that Deg1 cooperates with the stroma-exposed proteases FtsH and Deg2 in degrading D1 protein during repair from photoinhibition by cleaving lumen-exposed regions of the protein. In addition, they suggest that accumulation of Deg1 and FtsH proteases may be coordinated.

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“…A homozygous line of the mutant was isolated (Fig. 6B) that was unable to transcribe the DEG15 gene as shown by reverse transcription (RT)-PCR using the DEG2 gene, encoding a chloroplast DEG2 protein (Haussuhl et al, 2001;Huesgen et al, 2006), as a control (Fig. 6C).…”

Section: The Range Of Proteins Processed By Deg15mentioning

confidence: 99%

The DEG15 Serine Protease Cleaves Peroxisomal Targeting Signal 2-Containing Proteins in Arabidopsis

et al. 2008

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Two distinct peroxisomal targeting signals (PTSs), the C-terminal PTS1 and the N-terminal PTS2, are defined. Processing of the PTS2 on protein import is conserved in higher eukaryotes. Recently, candidates for the responsible processing protease were identified from plants (DEG15) and mammals (TYSND1). We demonstrate that plants lacking DEG15 show an expressed phenotype potentially linked to reduced b-oxidation, indicating the impact of protein processing on peroxisomal functions in higher eukaryotes. Mutational analysis of Arabidopsis (Arabidopsis thaliana) DEG15 revealed that conserved histidine, aspartic acid, and serine residues are essential for the proteolytic activity of this enzyme in vitro. This indicates that DEG15 and related enzymes are trypsin-like serine endopeptidases. Deletion of a plant-specific stretch present in the protease domain diminished, but did not abolish, the proteolytic activity of DEG15 against the PTS2-containing glyoxysomal malate dehydrogenase. Fluorescence microscopy showed that a DEG15-green fluorescent protein fusion construct is targeted to peroxisomes in planta. In vivo studies with isolated homozygous deg15 knockout mutants and complemented mutant lines suggest that this enzyme mediates general processing of PTS2-containing proteins.

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Photodamaged D1 protein is degraded in Arabidopsis mutants lacking the Deg2 protease

Cited by 57 publications

References 32 publications

The Phosphorylation Status of the Chloroplast Protein Kinase STN7 of Arabidopsis Affects Its Turnover

The Phosphorylation Status of the Chloroplast Protein Kinase STN7 of Arabidopsis Affects Its Turnover

The Thylakoid Lumen Protease Deg1 Is Involved in the Repair of Photosystem II from Photoinhibition in Arabidopsis

The DEG15 Serine Protease Cleaves Peroxisomal Targeting Signal 2-Containing Proteins in Arabidopsis

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