ArticleBMC biochemistry2009
The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains.
Article in BMC biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Assembly of two functionally-distinct protein import complexes in the outer membrane of plant chloroplasts.Nature communications · 2026Article
- Split-Ubiquitin Two-Hybrid Screen for Proteins Interacting with slToc159-1 and slToc159-2, Two Chloroplast Preprotein Import Receptors in Tomato (Plants (Basel, Switzerland) · 2022Article
- DispHred: A Server to Predict pH-Dependent Order-Disorder Transitions in Intrinsically Disordered Proteins.International journal of molecular sciences · 2020Article
- Article
- The novel chloroplast outer membrane kinase KOC1 is a required component of the plastid protein import machinery.The Journal of biological chemistry · 2017Article
- Import of Soluble Proteins into Chloroplasts and Potential Regulatory Mechanisms.Frontiers in plant science · 2017Review
- Folding and self-association of atTic20 in lipid membranes: implications for understanding protein transport across the inner envelope membrane of chloroplasts.BMC biochemistry · 2014Article
- Targeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane.Frontiers in plant science · 2014Review
- Article
- Molecular characterization and expression analysis of chloroplast protein import components in tomato (Solanum lycopersicum).PloS one · 2014Article
- Border control: selectivity of chloroplast protein import and regulation at the TOC-complex.Frontiers in plant science · 2014Review
- The C-terminus of Bienertia sinuspersici Toc159 contains essential elements for its targeting and anchorage to the chloroplast outer membrane.Frontiers in plant science · 2014Article
- A transit peptide-like sorting signal at the C terminus directs the Bienertia sinuspersici preprotein receptor Toc159 to the chloroplast outer membrane.The Plant cell · 2012Article
- Phosphorylation of intrinsically disordered regions in remorin proteins.Frontiers in plant science · 2012Article
- Plastid proteome assembly without Toc159: photosynthetic protein import and accumulation of N-acetylated plastid precursor proteins.The Plant cell · 2011Article
- Modifications at the A-domain of the chloroplast import receptor Toc159.Plant signaling & behavior · 2010Article
- Iron-mediated oxidation induces conformational changes within the redox-sensing protein HbpS.The Journal of biological chemistry · 2010Article
- The acidic A-domain of Arabidopsis TOC159 occurs as a hyperphosphorylated protein.Plant physiology · 2010Article
- The molecular basis for distinct pathways for protein import into Arabidopsis chloroplasts.The Plant cell · 2010Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Toc159 family of proteins serve as receptors for chloroplast-destined preproteins. They directly bind to transit peptides, and exhibit preprotein substrate selectivity conferred by an unknown mechanism. The Toc159 receptors each include three domains: C-terminal membrane, central GTPase, and N-terminal acidic (A-) domains. Although the function(s) of the A-domain remains largely unknown, the amino acid sequences are most variable within these domains, suggesting they may contribute to the functional specificity of the receptors.
resultsThe physicochemical properties of the A-domains are characteristic of intrinsically disordered proteins (IDPs). Using CD spectroscopy we show that the A-domains of two Arabidopsis Toc159 family members (atToc132 and atToc159) are disordered at physiological pH and temperature and undergo conformational changes at temperature and pH extremes that are characteristic of IDPs.
conclusionsIdentification of the A-domains as IDPs will be important for determining their precise function(s), and suggests a role in protein-protein interactions, which may explain how these proteins serve as receptors for such a wide variety of preprotein substrates.
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