ArticleThe Plant journal : for cell and molecular biology2013
Structural characterizations of the chloroplast translocon protein Tic110.
Article in The Plant journal : for cell and molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Correlated Evolutionary Rates Reveal Novel Components and Cross-Compartment Connectivity in Plant Proteostasis Systems.Genome biology and evolution · 2026Article
- Plant plastids: from evolutionary origins to functional specialization and organelle interactions.Journal of experimental botany · 2025Review
- Biparental plastid inheritance and its implications in plastid genome engineering.Plant cell reports · 2025Review
- Understanding protein import in diverse non-green plastids.Frontiers in genetics · 2023Review
- Chloroplast protein import machinery and quality control.The FEBS journal · 2022Review
- Mutations in the chloroplast inner envelope protein TIC100 impair and repair chloroplast protein import and impact retrograde signaling.The Plant cell · 2022Article
- Genetic Mapping of theFrontiers in plant science · 2022Article
- Gene introduction approaches in chloroplast transformation and its applications.Journal, genetic engineering & biotechnology · 2021Review
- Coexpressed subunits of dual genetic origin define a conserved supercomplex mediating essential protein import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Origins, function, and regulation of the TOC-TIC general protein import machinery of plastids.Journal of experimental botany · 2020Article
- ARSENATE INDUCED CHLOROSIS 1/ TRANSLOCON AT THE OUTER ENVOLOPE MEMBRANE OF CHLOROPLASTS 132 Protects Chloroplasts from Arsenic Toxicity.Plant physiology · 2018Article
- En route into chloroplasts: preproteins' way home.Photosynthesis research · 2018Review
- The integration of chloroplast protein targeting with plant developmental and stress responses.BMC biology · 2017Review
- Suppressors of the Chloroplast Protein Import MutantThe Plant cell · 2017Article
- Import of Soluble Proteins into Chloroplasts and Potential Regulatory Mechanisms.Frontiers in plant science · 2017Review
- Synthesis and transfer of galactolipids in the chloroplast envelope membranes of Arabidopsis thaliana.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Functional Analysis of the Hsp93/ClpC Chaperone at the Chloroplast Envelope.Plant physiology · 2016Article
- Sequence Motifs in Transit Peptides Act as Independent Functional Units and Can Be Transferred to New Sequence Contexts.Plant physiology · 2015Article
- The complexity, challenges and benefits of comparing two transporter classification systems in TCDB and Pfam.Briefings in bioinformatics · 2015Article
- New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Journal of molecular biology · 2015Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tic110 is a major component of the chloroplast protein import translocon. Two functions with mutually exclusive structures have been proposed for Tic110: a protein-conducting channel with six transmembrane domains and a scaffold with two N-terminal transmembrane domains followed by a large soluble domain for binding transit peptides and other stromal translocon components. To investigate the structure of Tic110, Tic110 from Cyanidioschyzon merolae (CmTic110) was characterized. We constructed three fragments, CmTic110A , CmTic110B and CmTic110C , with increasing N-terminal truncations, to perform small-angle X-ray scattering (SAXS) and X-ray crystallography analyses and Dali structural comparison. Here we report the molecular envelope of CmTic110B and CmTic110C determined by SAXS, and the crystal structure of CmTic110C at 4.2 Å. Our data indicate that the C-terminal half of CmTic110 possesses a rod-shaped helix-repeat structure that is too flattened and elongated to be a channel. The structure is most similar to the HEAT-repeat motif that functions as scaffolds for protein-protein interactions.
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