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Structural Analysis and Molecular Model of a Self-Incompatibility RNase from Wild Tomato1

Simon Parry, Ed Newbigin, David Craik, Kazuo T. Nakamura, Antony Bacic*, and David Oxley

Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, VIC 3052, Australia (S.P., E.N., A.B., D.O.); Centre for Drug Design and Development, University of Queensland, QLD 4072, Australia (D.C.); and School of Pharmaceutical Sciences, Showa University, Hatanodai, Tokyo 142, Japan (K.T.N.)

Self-incompatibility RNases (S-RNases) are an allelic series of style glycoproteins associated with rejection of self-pollen in solanaceous plants. The nucleotide sequences of S-RNase alleles from several genera have been determined, but the structure of the gene products has only been described for those from Nicotiana alata. We report on the N-glycan structures and the disulfide bonding of the S3-RNase from wild tomato (Lycopersicon peruvianum) and use this and other information to construct a model of this molecule. The S3-RNase has a single N-glycosylation site (Asn-28) to which one of three N-glycans is attached. S3-RNase has seven Cys residues; six are involved in disulfide linkages (Cys-16-Cys-21, Cys-46-Cys-91, and Cys-166-Cys-177), and one has a free thiol group (Cys-150). The disulfide-bonding pattern is consistent with that observed in RNase Rh, a related RNase for which radiographic-crystallographic information is available. A molecular model of the S3-RNase shows that four of the most variable regions of the S-RNases are clustered on one surface of the molecule. This is discussed in the context of recent experiments that set out to determine the regions of the S-RNase important for recognition during the self-incompatibility response.

1   This work was supported by a Special Research Centre grant from the Australian Research Council. We acknowledge support for the purchase of the electrospray-ionization mass spectrometer from the Clive and Vera Ramaciotti Foundations, the Ian Potter Foundation, The Australian Research Council, and the University of Melbourne. S.P. is the recipient of a Melbourne University Scholarship from the Faculty of Science and School of Botany.
*   Corresponding author; e-mail antony_bacic{at}mac.unimelb.edu.au; fax 61-3-9347-1071.

Plant Physiol. (1998) 116: 463-469
Copyright Clearance Center:   0032-0889/98/116/0463/07
© 1998 American Society of Plant Physiologists




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