The acidic domains of the Toc159 chloroplast preprotein receptor family are intrinsically disordered protein domains |
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| Authors: | Lynn GL Richardson Masoud Jelokhani-Niaraki Matthew D Smith |
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| Institution: | (1) Department of Biology, Wilfrid Laurier University, Waterloo, ON, N2L 3C5, Canada;(2) Department of Biology, University of Waterloo, Waterloo, ON, N2L 3G1, Canada;(3) Department of Chemistry, Wilfrid Laurier University, Waterloo, ON, N2L 3C5, Canada;(4) Department of Molecular and Cellular Biology, University of Guelph, Guelph, ON, Canada |
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| Abstract: | Background The 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. |
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