Molecular determinants of protein half-life in chloroplasts with focus on the Clp protease system
Author:
Winckler Lioba Inken123, Dissmeyer Nico123ORCID
Affiliation:
1. Department of Plant Physiology and Protein Metabolism Laboratory , University of Osnabruck , Barbarastrasse 11, D-49076 Osnabruck , Germany 2. Center of Cellular Nanoanalytics (CellNanOs) , Barbarastrasse 11, D-49076 Osnabruck , Germany 3. Faculty of Biology , University of Osnabruck , Barbarastrasse 11, D-49076 Osnabruck , Germany
Abstract
Abstract
Proteolysis is an essential process to maintain cellular homeostasis. One pathway that mediates selective protein degradation and which is in principle conserved throughout the kingdoms of life is the N-degron pathway, formerly called the ‘N-end rule’. In the cytosol of eukaryotes and prokaryotes, N-terminal residues can be major determinants of protein stability. While the eukaryotic N-degron pathway depends on the ubiquitin proteasome system, the prokaryotic counterpart is driven by the Clp protease system. Plant chloroplasts also contain such a protease network, which suggests that they might harbor an organelle specific N-degron pathway similar to the prokaryotic one. Recent discoveries indicate that the N-terminal region of proteins affects their stability in chloroplasts and provides support for a Clp-mediated entry point in an N-degron pathway in plastids. This review discusses structure, function and specificity of the chloroplast Clp system, outlines experimental approaches to test for an N-degron pathway in chloroplasts, relates these aspects into general plastid proteostasis and highlights the importance of an understanding of plastid protein turnover.
Funder
Deutsche Forschungsgemeinschaft European Regional Development Fund
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Reference120 articles.
1. Adam, Z., Adamska, I., Nakabayashi, K., Ostersetzer, O., Haussuhl, K., Manuell, A., Zheng, B., Vallon, O., Rodermel, S.R., Shinozaki, K., et al.. (2001). Chloroplast and mitochondrial proteases in Arabidopsis. A proposed nomenclature. Plant Physiol. 125: 1912–1918, https://doi.org/10.1104/pp.125.4.1912. 2. Aguilar Lucero, D., Cantoia, A., Sanchez-Lopez, C., Binolfi, A., Mogk, A., Ceccarelli, E.A., and Rosano, G.L. (2021). Structural features of the plant N-recognin ClpS1 and sequence determinants in its targets that govern substrate selection. FEBS Lett. 595: 1525–1541, https://doi.org/10.1002/1873-3468.14081. 3. Ahyoung, A.P., Koehl, A., Vizcarra, C.L., Cascio, D., and Egea, P.F. (2016). Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogen Plasmodium falciparum. Protein Sci. 25: 689–701, https://doi.org/10.1002/pro.2868. 4. Apel, W., Schulze, W.X., and Bock, R. (2010). Identification of protein stability determinants in chloroplasts. Plant J. 63: 636–650, https://doi.org/10.1111/j.1365-313x.2010.04268.x. 5. Apitz, J., Nishimura, K., Schmied, J., Wolf, A., Hedtke, B., Van Wijk, K.J., and Grimm, B. (2016). Posttranslational control of ALA synthesis includes GluTR degradation by Clp protease and stabilization by GluTR-binding protein. Plant Physiol. 170: 2040–2051, https://doi.org/10.1104/pp.15.01945.
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