ArticleThe Plant journal : for cell and molecular biology2011
FtsH2 and FtsH5: two homologous subunits use different integration mechanisms leading to the same thylakoid multimeric complex.
Article in The Plant journal : for cell and molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- A FtsH-Like Zinc Metalloprotease, OsFtsH1, Coordinates Chloroplast Development and Photosystem II Homeostasis in Rice.Rice (New York, N.Y.) · 2026Article
- The Transmembrane Glutamate Serves as a pH Sensor for Tha4 Oligomerization During Twin Arginine Transport of Proteins.Plants (Basel, Switzerland) · 2025Article
- Temperature-driven changes in membrane fluidity differentially impact FILAMENTATION TEMPERATURE-SENSITIVE H2-mediated photosystem II repair.The Plant cell · 2024Article
- MFP1 defines the subchloroplast location of starch granule initiation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Silencing of PepperInternational journal of molecular sciences · 2023Article
- Recent Advances in Understanding the Structural and Functional Evolution of FtsH Proteases.Frontiers in plant science · 2022Review
- Current Understanding of Temperature Stress-Responsive Chloroplast FtsH Metalloproteases.International journal of molecular sciences · 2021Review
- Membrane Chaperoning of a Thylakoid Protease Whose Structural Stability Is Modified by the Protonmotive Force.The Plant cell · 2020Article
- Two paths diverged in the stroma: targeting to dual SEC translocase systems in chloroplasts.Photosynthesis research · 2018Review
- FtsH Protease in the Thylakoid Membrane: Physiological Functions and the Regulation of Protease Activity.Frontiers in plant science · 2018Review
- A Plastid Phosphatidylglycerol Lipase Contributes to the Export of Acyl Groups from Plastids for Seed Oil Biosynthesis.The Plant cell · 2017Article
- Identification of Putative Substrates of SEC2, a Chloroplast Inner Envelope Translocase.Plant physiology · 2017Article
- Integrated Physiological, Proteomic, and Metabolomic Analysis of Ultra Violet (UV) Stress Responses and Adaptation Mechanisms inMolecular & cellular proteomics : MCP · 2017Article
- Chloroplast Proteases: Updates on Proteolysis within and across Suborganellar Compartments.Plant physiology · 2016Review
- Article
- Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1.The Journal of biological chemistry · 2015Article
- Thylakoid FtsH protease contributes to photosystem II and cytochrome b6f remodeling in Chlamydomonas reinhardtii under stress conditions.The Plant cell · 2014Article
- Understanding chloroplast biogenesis using second-site suppressors of immutans and var2.Photosynthesis research · 2013Review
- Intra-plastid protein trafficking: how plant cells adapted prokaryotic mechanisms to the eukaryotic condition.Biochimica et biophysica acta · 2013Review
- Cooperative D1 degradation in the photosystem II repair mediated by chloroplastic proteases in Arabidopsis.Plant physiology · 2012Article
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3 authors.
Funding
Abstract
The Arabidopsis thylakoid FtsH protease complex is composed of FtsH1/FtsH5 (type A) and FtsH2/FtsH8 (type B) subunits. Type A and type B subunits display a high degree of sequence identity throughout their mature domains, but no similarity in their amino-terminal targeting peptide regions. In chloroplast import assays, FtsH2 and FtsH5 were imported and subsequently integrated into thylakoids by a two-step processing mechanism that resulted in an amino-proximal lumenal domain, a single transmembrane anchor, and a carboxyl proximal stromal domain. FtsH2 integration into washed thylakoids was entirely dependent on the proton gradient, whereas FtsH5 integration was dependent on NTPs, suggesting their integration by Tat and Sec pathways, respectively. This finding was corroborated by in organello competition and by antibody inhibition experiments. A series of constructs were made in order to understand the molecular basis for different integration pathways. The amino proximal domains through the transmembrane anchors were sufficient for proper integration as demonstrated with carboxyl-truncated versions of FtsH2 and FtsH5. The mature FtsH2 protein was found to be incompatible with the Sec machinery as determined with targeting peptide-swapping experiments. Incompatibility does not appear to be determined by any specific element in the FtsH2 domain as no single domain was incompatible with Sec transport. This suggests an incompatible structure that requires the intact FtsH2. That the highly homologous type A and type B subunits of the same multimeric complex use different integration pathways is a striking example of the notion that membrane insertion pathways have evolved to accommodate structural features of their respective substrates.
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