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Plant Cell, Vol. 12, 493-506, April 2000, Copyright © 2000, American Society of Plant Physiologists

Structural Requirements for Ligand Binding by a Probable Plant Vacuolar Sorting Receptor

Xiaofeng Caoa, Sally W. Rogersa, Juliet Butlerb, Leonard Beeversb, and John C. Rogersa
a Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340
b Botany and Microbiology Department, University of Oklahoma, Norman, Oklahoma 73019-0001

Correspondence to: John C. Rogers, bcjroger{at}wsu.edu (E-mail), 509-335-7643 (fax)

How sorting receptors recognize amino acid determinants on polypeptide ligands and respond to pH changes for ligand binding or release is unknown. The plant vacuolar sorting receptor BP-80 binds polypeptide ligands with a central Asn-Pro-Ile-Arg (NPIR) motif. tBP-80, a soluble form of the receptor lacking transmembrane and cytoplasmic sequences, binds the peptide SSSFADSNPIRPVTDRAASTYC as a monomer with a specificity indistinguishable from that of BP-80. tBP-80 contains an N-terminal region homologous to ReMembR-H2 (RMR) protein lumenal domains, a unique central region, and three C-terminal epidermal growth factor (EGF) repeats. By protease digestion of purified secreted tBP-80, and from ligand binding studies with a secreted protein lacking the EGF repeats, we defined three protease-resistant structural domains: an N-terminal/RMR homology domain connected to a central domain, which together determine the NPIR-specific ligand binding site, and a C-terminal EGF repeat domain that alters the conformation of the other two domains to enhance ligand binding. A fragment representing the central domain plus the C-terminal domain could bind ligand but was not specific for NPIR. These results indicate that two tBP-80 binding sites recognize two separate ligand determinants: a non-NPIR site defined by the central domain–EGF repeat domain structure and an NPIR-specific site contributed by the interaction of the N-terminal/RMR homology domain and the central domain.




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