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Takechi, K.1
Sodmergen2
Murata, M.3
Motoyoshi, F.4
Sakamoto, W.5
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39
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0036668462
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The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is responsible for leaf variegation in the mutant alleles
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Sakamoto W., Tamura T., Hanba-Tomita Y., Sodmergen, and Murata M. The VAR1 locus of Arabidopsis encodes a chloroplastic FtsH and is responsible for leaf variegation in the mutant alleles. Genes Cells 7 (2002) 769-780
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Sakamoto, W.1
Tamura, T.2
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Sodmergen4
Murata, M.5
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40
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20444444744
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Developmental and light effects on the accumulation of FtsH protease in Arabidopsis chloroplasts - implications for thylakoid formation and photosystem II maintenance
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The authors use the FtsH2 mutant to show that FtsH expression increases during development, leading to a decreased proportion of white sectors in the variegated leaves of the mutant. They also demonstrate that the level of FtsH decreases during the initial stages of exposure to high light, an effect that is reversed by the increase in FtsH transcript level under high light.
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Zaltsman A., Feder A., and Adam Z. Developmental and light effects on the accumulation of FtsH protease in Arabidopsis chloroplasts - implications for thylakoid formation and photosystem II maintenance. Plant J 42 (2005) 609-617. The authors use the FtsH2 mutant to show that FtsH expression increases during development, leading to a decreased proportion of white sectors in the variegated leaves of the mutant. They also demonstrate that the level of FtsH decreases during the initial stages of exposure to high light, an effect that is reversed by the increase in FtsH transcript level under high light.
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Plant J
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Zaltsman, A.1
Feder, A.2
Adam, Z.3
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41
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Two types of FtsH protease subunits are required for chloroplast biogenesis and Photosystem II repair in Arabidopsis
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A series of FtsH double mutants established the relations between the different subunits of the complex. Mutations in FtsH1 and FtsH8 enhanced the phenotypes of the FtsH5 and FtsH2 mutants, respectively, resulting in albino seedlings. These results suggested that it is essential for the FtsH complex to contain representatives from the two pairs of the duplicated genes (FtsH1 plus FtsH5 and FtsH2 plus FtsH8) but that genes within a pair are redundant.
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Zaltsman A., Ori N., and Adam Z. Two types of FtsH protease subunits are required for chloroplast biogenesis and Photosystem II repair in Arabidopsis. Plant Cell 17 (2005) 2782-2790. A series of FtsH double mutants established the relations between the different subunits of the complex. Mutations in FtsH1 and FtsH8 enhanced the phenotypes of the FtsH5 and FtsH2 mutants, respectively, resulting in albino seedlings. These results suggested that it is essential for the FtsH complex to contain representatives from the two pairs of the duplicated genes (FtsH1 plus FtsH5 and FtsH2 plus FtsH8) but that genes within a pair are redundant.
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Plant Cell
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Zaltsman, A.1
Ori, N.2
Adam, Z.3
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42
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AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence
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Zelisko A., Garcia-Lorenzo M., Jackowski G., Jansson S., and Funk C. AtFtsH6 is involved in the degradation of the light-harvesting complex II during high-light acclimation and senescence. Proc Natl Acad Sci USA 102 (2005) 13699-13704
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Zelisko, A.1
Garcia-Lorenzo, M.2
Jackowski, G.3
Jansson, S.4
Funk, C.5
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43
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0031153994
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Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: the possible role of the FtsH protease
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Ostersetzer O., and Adam Z. Light-stimulated degradation of an unassembled Rieske FeS protein by a thylakoid-bound protease: the possible role of the FtsH protease. Plant Cell 9 (1997) 957-965
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Ostersetzer, O.1
Adam, Z.2
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44
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The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein
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Lindahl M., Spetea C., Hundal T., Oppenheim A.B., Adam Z., and Andersson B. The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein. Plant Cell 12 (2000) 419-431
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Lindahl, M.1
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Oppenheim, A.B.4
Adam, Z.5
Andersson, B.6
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45
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0037127195
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A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo
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Bailey S., Thompson E., Nixon P.J., Horton P., Mullineaux C.W., Robinson C., and Mann N.H. A critical role for the Var2 FtsH homologue of Arabidopsis thaliana in the photosystem II repair cycle in vivo. J Biol Chem 277 (2002) 2006-2011
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Bailey, S.1
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Mullineaux, C.W.5
Robinson, C.6
Mann, N.H.7
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46
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FtsH-mediated repair of the photosystem II complex in response to light stress
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Nixon P.J., Barker M., Boehm M., de Vries R., and Komenda J. FtsH-mediated repair of the photosystem II complex in response to light stress. J Exp Bot 56 (2005) 357-363
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Komenda, J.5
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47
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Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in thylakoid membrane biogenesis
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This study establishes a link between the thylakoid-bound FtsH proteins and ClpC chaperones for the first time. It opens up exciting avenues for further research into chloroplast protease networks.
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Park S., and Rodermel S.R. Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in thylakoid membrane biogenesis. Proc Natl Acad Sci USA 101 (2004) 12765-12770. This study establishes a link between the thylakoid-bound FtsH proteins and ClpC chaperones for the first time. It opens up exciting avenues for further research into chloroplast protease networks.
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Proc Natl Acad Sci USA
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Park, S.1
Rodermel, S.R.2
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Function of the stromal processing peptidase in the chloroplast import pathway
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Richter S., and Lamppa G. Function of the stromal processing peptidase in the chloroplast import pathway. Physiol Plant 123 (2005) 362-368
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Richter, S.1
Lamppa, G.2
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21144447897
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Two novel targeting peptide degrading proteases, PrePs, in mitochondria and chloroplasts, so similar and still different
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Stahl A., Nilsson S., Lundberg P., Bhushan S., Biverstahl H., Moberg P., Morisset M., Vener A., Maler L., Langel U., et al. Two novel targeting peptide degrading proteases, PrePs, in mitochondria and chloroplasts, so similar and still different. J Mol Biol 349 (2005) 847-860
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Stahl, A.1
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Morisset, M.7
Vener, A.8
Maler, L.9
Langel, U.10
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50
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Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts
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Moberg P., Stahl A., Bhushan S., Wright S.J., Eriksson A., Bruce B.D., and Glaser E. Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts. Plant J 36 (2003) 616-628
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Bruce, B.D.6
Glaser, E.7
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51
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Catalysis, subcellular localization, expression and evolution of the targeting peptides degrading protease, AtPreP2
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Bhushan S., Stahl A., Nilsson S., Lefebvre B., Seki M., Roth C., McWilliam D., Wright S.J., Liberles D.A., Shinozaki K., et al. Catalysis, subcellular localization, expression and evolution of the targeting peptides degrading protease, AtPreP2. Plant Cell Physiol 46 (2005) 985-996
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McWilliam, D.7
Wright, S.J.8
Liberles, D.A.9
Shinozaki, K.10
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52
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27744459930
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Complete maturation of the plastid protein translocation channel requires a type I signal peptidase
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Maturation of the Toc75 plastid translocation channel is required for its function. This work demonstrates that a type I signal peptidase, located in the inner envelope membrane, is responsible for this process. Disruption of the gene that encodes this peptidase results in the accumulation of an intermediate form of Toc75 and seedling lethality. This is the first protease identified in the envelope.
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Inoue K., Baldwin A.J., Shipman R.L., Matsui K., Theg S.M., and Ohme-Takagi M. Complete maturation of the plastid protein translocation channel requires a type I signal peptidase. J Cell Biol 171 (2005) 425-430. Maturation of the Toc75 plastid translocation channel is required for its function. This work demonstrates that a type I signal peptidase, located in the inner envelope membrane, is responsible for this process. Disruption of the gene that encodes this peptidase results in the accumulation of an intermediate form of Toc75 and seedling lethality. This is the first protease identified in the envelope.
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J Cell Biol
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Inoue, K.1
Baldwin, A.J.2
Shipman, R.L.3
Matsui, K.4
Theg, S.M.5
Ohme-Takagi, M.6
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53
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11144322224
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The DNA-binding protease, CND41, and the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase in senescent leaves of tobacco
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Kato Y., Murakami S., Yamamoto Y., Chatani H., Kondo Y., Nakano T., Yokota A., and Sato F. The DNA-binding protease, CND41, and the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase in senescent leaves of tobacco. Planta 220 (2004) 97-104
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Kato, Y.1
Murakami, S.2
Yamamoto, Y.3
Chatani, H.4
Kondo, Y.5
Nakano, T.6
Yokota, A.7
Sato, F.8
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54
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Post-translational regulation of CND41 protease activity in senescent tobacco leaves
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Kato Y., Yamamoto Y., Murakami S., and Sato F. Post-translational regulation of CND41 protease activity in senescent tobacco leaves. Planta 222 (2005) 643-651
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Kato, Y.1
Yamamoto, Y.2
Murakami, S.3
Sato, F.4
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