The major peptidyl‐prolyl isomerase activity in thylakoid lumen of plant chloroplasts belongs to a novel cyclophilin TLP20

Edvardsson, Anna; Eshaghi, Said; Vener, Alexander V.; Andersson, Bertil

doi:10.1016/s0014-5793(03)00366-1

Cited by 40 publications

(40 citation statements)

References 25 publications

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“…Several proteins identified in maize and Arabidopsis NDH complexes by proteomics analysis (Majeran et al, 2008;Sirpiö et al, 2009a) were detected and classified into the third group. CYP20-2 (Tlp20), which was recently shown to be an auxiliary subunit of the NDH complex (Sirpiö et al, 2009b), is a peptidyl-prolyl cis/trans isomerase of 20 kD present in the thylakoid lumen (Edvardsson et al, 2003). FKBP16-2, two PsbQ family proteins (PsbQ-F1 and PsbQ-F2), and transmembrane protein NDH18 were also detected (Table 1).…”

Section: Mass Analysis Of the Ndh-psi Supercomplexmentioning

confidence: 99%

Efficient Operation of NAD(P)H Dehydrogenase Requires Supercomplex Formation with Photosystem I via Minor LHCI in Arabidopsis

et al. 2009

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In higher plants, the chloroplast NAD(P)H dehydrogenase (NDH) complex mediates photosystem I (PSI) cyclic and chlororespiratory electron transport. We reported previously that NDH interacts with the PSI complex to form a supercomplex (NDH-PSI). In this study, NDH18 and FKBP16-2 (FK506 Binding Protein 16-2), detected in the NDH-PSI supercomplex by mass spectrometry, were shown to be NDH subunits by the analysis of their knockdown lines. On the basis of extensive mutant characterization, we propose a structural model for chloroplast NDH, whereby NDH is divided into four subcomplexes. The subcomplex A and membrane subcomplex are conserved in cyanobacteria, but the subcomplex B and lumen subcomplex are specific to chloroplasts. Two minor light-harvesting complex I proteins, Lhca5 and Lhca6, were required for the full-size NDH-PSI supercomplex formation. Similar to crr pgr5 double mutants that completely lack cyclic electron flow activity around PSI, the lhca6 pgr5 double mutant exhibited a severe defect in growth. Consistent with the impaired NDH activity, photosynthesis was also severely affected in mature leaves of lhca6 pgr5. We conclude that chloroplast NDH became equipped with the novel subcomplexes and became associated with PSI during the evolution of land plants, and this process may have facilitated the efficient operation of NDH.

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Section: Mass Analysis Of the Ndh-psi Supercomplexmentioning

confidence: 99%

Efficient Operation of NAD(P)H Dehydrogenase Requires Supercomplex Formation with Photosystem I via Minor LHCI in Arabidopsis

et al. 2009

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“…All of the isomerases are located on the lumenal side of the thylakoid membrane and they might have a variety of functions, from folding of proteins to signaling (Fulgosi et al, 1998;Edvardsson et al, 2003). cpSecE is a component of the SecY/E translocon involved in the translocation of a subset of lumenal proteins as well as integral thylakoid membrane proteins (Schuenemann et al, 1999).…”

Section: Chaperones Protein Assembly Insertion Proteolysis and Ismentioning

confidence: 99%

In-Depth Analysis of the Thylakoid Membrane Proteome ofArabidopsis thalianaChloroplasts: New Proteins, New Functions, and a Plastid Proteome Database[W]

et al. 2004

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An extensive analysis of the Arabidopsis thaliana peripheral and integral thylakoid membrane proteome was performed by sequential extractions with salt, detergent, and organic solvents, followed by multidimensional protein separation steps (reverse-phase HPLC and one-and two-dimensional electrophoresis gels), different enzymatic and nonenzymatic protein cleavage techniques, mass spectrometry, and bioinformatics. Altogether, 154 proteins were identified, of which 76 (49%) were a-helical integral membrane proteins. Twenty-seven new proteins without known function but with predicted chloroplast transit peptides were identified, of which 17 (63%) are integral membrane proteins. These new proteins, likely important in thylakoid biogenesis, include two rubredoxins, a potential metallochaperone, and a new DnaJ-like protein. The data were integrated with our analysis of the lumenal-enriched proteome. We identified 83 out of 100 known proteins of the thylakoid localized photosynthetic apparatus, including several new paralogues and some 20 proteins involved in protein insertion, assembly, folding, or proteolysis. An additional 16 proteins are involved in translation, demonstrating that the thylakoid membrane surface is an important site for protein synthesis. The high coverage of the photosynthetic apparatus and the identification of known hydrophobic proteins with low expression levels, such as cpSecE, Ohp1, and Ohp2, indicate an excellent dynamic resolution of the analysis. The sequential extraction process proved very helpful to validate transmembrane prediction. Our data also were cross-correlated to chloroplast subproteome analyses by other laboratories. All data are deposited in a new curated plastid proteome database (PPDB) with multiple search functions (http:// cbsusrv01.tc.cornell.edu/users/ppdb/). This PPDB will serve as an expandable resource for the plant community.

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“…Although AtCYP20-3 has been clearly identified as a stromal protein (Lippuner et al, 1994;Schubert et al, 2002), the inability of CsA to block import of Rubisco and the 33-kD subunit of the oxygen evolving complex in an in vitro import assay suggests that PPiase activity may not be involved in this process (although CsA access into the chloroplast in these experiments was not assessed). The SD isoform AtCYP20-2 and its spinach homolog TLP20 have been shown to possess CsA-sensitive PPiase activity (Edvardsson et al, 2003;P.G.N. Romano, unpublished data), and have been isolated from both lumenal and thylakoid membrane fractions (Peltier et al, 2002;Schubert et al, 2002;Edvardsson et al, 2003), suggesting that this protein may be recruited to the membrane as part of its function.…”

Section: Chloroplast Cyclophilinsmentioning

confidence: 99%

The Arabidopsis Cyclophilin Gene Family

2004

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Database searching has allowed the identification of a number of previously unreported single and multidomain isoform members of the Arabidopsis cyclophilin gene family. In addition to the cyclophilin-like peptidyl-prolyl cis-trans isomerase domain, the latter contain a variety of other domains with characterized functions. Transcriptional analysis showed they are expressed throughout the plant, and different isoforms are present in all parts of the cell including the cytosol, nucleus, mitochondria, secretory pathway, and chloroplast. The abundance and diversity of cyclophilin isoforms suggests that, like their animal counterparts, plant cyclophilins are likely to be important proteins involved in a wide variety of cellular processes. As well as fulfilling the basic role of protein folding, they may also play important roles in mRNA processing, protein degradation, and signal transduction and thus may be crucial during both development and stress responsiveness.

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The major peptidyl‐prolyl isomerase activity in thylakoid lumen of plant chloroplasts belongs to a novel cyclophilin TLP20

Cited by 40 publications

References 25 publications

Efficient Operation of NAD(P)H Dehydrogenase Requires Supercomplex Formation with Photosystem I via Minor LHCI in Arabidopsis

Efficient Operation of NAD(P)H Dehydrogenase Requires Supercomplex Formation with Photosystem I via Minor LHCI in Arabidopsis

In-Depth Analysis of the Thylakoid Membrane Proteome ofArabidopsis thalianaChloroplasts: New Proteins, New Functions, and a Plastid Proteome Database[W]

The Arabidopsis Cyclophilin Gene Family

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