The family of Deg proteases in cyanobacteria and chloroplasts of higher plants

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

doi:10.1111/j.1399-3054.2005.00458.x

Cited by 64 publications

(90 citation statements)

References 45 publications

(81 reference statements)

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“…Photoinhibition on either the donor side or the acceptor side may trigger the damage and subsequent degradation of PSII proteins, particularly the D1 protein (Andersson and Aro, 2001;Huesgen et al, 2005). In acceptor-side photoinhibition, the primary cleavage of the D1 protein appears to occur in the stromal loop connecting the transmembrane helices D and E, based on the detection of 23-kD N-terminal and 10-kD C-terminal fragments in samples examined by various authors (Greenberg et al, 1987;Canovas and Barber, 1993;Shipton and Barber, 1994;Kanervo et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Formation of DEG5 and DEG8 Complexes and Their Involvement in the Degradation of Photodamaged Photosystem II Reaction Center D1 Protein in Arabidopsis

et al. 2007

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The widely distributed DEGP proteases play important roles in the degradation of damaged and misfolded proteins. Arabidopsis thaliana contains 16 DEGP-like proteases, four of which are located in the chloroplast. Here, we show that DEG5 and DEG8 form a hexamer in the thylakoid lumen and that recombinant DEG8 is proteolytically active toward both a model substrate (b-casein) and photodamaged D1 protein of photosystem II (PSII), producing 16-kD N-terminal and 18-kD C-terminal fragments. Inactivation of DEG5 and DEG8 resulted in increased sensitivity to photoinhibition. Turnover of newly synthesized D1 protein in the deg5 deg8 double mutant was impaired, and the degradation of D1 in the presence of the chloroplast protein synthesis inhibitor lincomycin under high-light treatment was slowed in the mutants. Thus, DEG5 and DEG8 are important for efficient turnover of the D1 protein and for protection against photoinhibition in vivo. The deg5 deg8 double mutant showed increased photosensitivity and reduced rates of D1 degradation compared with single mutants of deg5 and deg8. A 16-kD N-terminal degradation fragment of the D1 protein was detected in wild-type plants but not in the deg5 deg8 mutant following in vivo photoinhibition. Therefore, our results suggest that DEG5 and DEG8 have a synergistic function in the primary cleavage of the CD loop of the PSII reaction center protein D1.

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Section: Introductionmentioning

confidence: 99%

Formation of DEG5 and DEG8 Complexes and Their Involvement in the Degradation of Photodamaged Photosystem II Reaction Center D1 Protein in Arabidopsis

et al. 2007

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“…It should be noted that all Arabidopsis thaliana Deg proteins were initially designated DegPs. However, because Deg1, Deg5, and Deg8 are more closely related to each other than to their E. coli homologs, it was recently suggested that they be renamed Degs (Huesgen et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

“…Chloroplasts contain at least one more distantly related homolog, Deg2, peripherally attached to the stromal side of the thylakoid membrane (Haussuhl et al, 2001). Ten other plant homologs are predicted to reside in chloroplasts, mitochondria, and maybe other cellular sites (Huesgen et al, 2005). It should be noted that all Arabidopsis thaliana Deg proteins were initially designated DegPs.…”

Section: Introductionmentioning

confidence: 99%

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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“…However, MEROPS database gives also the other name -AtDegP2. All AtDeg proteases were originally named as AtDegPX ones and then renamed just AtDegX [11]. It has been shown recently that AtDeg2 exhibits chaperone-like activity in vitro [14] yet no data exist with regard to how protease and chaperone activities are interlocked within a single AtDeg2 molecule.…”

Section: Introductionmentioning

confidence: 99%

“…Sixteen genes coding for proteins orthologous to DegP, Q and S have been identified in the A. thaliana nuclear genome and designated AtDEG1-16 [11,12]. The genes code for proteins, which are targeted either to chloroplasts (AtDEG1, 2, 5, 7 and 8) or mitochondria (AtDEG10) or peroxisomes (AtDEG15).…”

Section: Introductionmentioning

confidence: 99%

AtDeg2 – a chloroplast protein with dual protease/chaperone activity

2014

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Chloroplast protease AtDeg2 (an ATP-independent serine endopeptidase) is cytosolically synthesized as a precursor, which is imported into the chloroplast stroma and deprived of its transit peptide. Then the mature protein undergoes routing to its functional location at the stromal side of thylakoid membrane. In its linear structure AtDeg2 molecule contains the protease domain with catalytic triad (HDS) and two PDZ domains (PDZ1 and PDZ2). In vivo AtDeg2 most probably exists as a supposedly inactive haxamer, which may change its oligomeric stage to form active 12-mer, or 24-mer. AtDeg2 has recently been demonstrated to exhibit dual protease/chaperone function. This review is focused on the current awareness with regard to AtDeg2 structure and functional significance.

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The family of Deg proteases in cyanobacteria and chloroplasts of higher plants

Cited by 64 publications

References 45 publications

Formation of DEG5 and DEG8 Complexes and Their Involvement in the Degradation of Photodamaged Photosystem II Reaction Center D1 Protein in Arabidopsis

Formation of DEG5 and DEG8 Complexes and Their Involvement in the Degradation of Photodamaged Photosystem II Reaction Center D1 Protein in Arabidopsis

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

AtDeg2 – a chloroplast protein with dual protease/chaperone activity

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