Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (26)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Parry, S.
Right arrow Articles by Oxley, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Parry, S.
Right arrow Articles by Oxley, D.
Agricola
Right arrow Articles by Parry, S.
Right arrow Articles by Oxley, D.

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




This article has been cited by other articles:


Home page
 GeneticsHome page
M. K. Uyenoyama, Y. Zhang, and E. Newbigin
On the Origin of Self-Incompatibility Haplotypes: Transition Through Self-Compatible Intermediates
Genetics, April 1, 2001; 157(4): 1805 - 1817.
[Abstract] [Full Text]

Home page
 Plant Physiol.Home page
E. J.M. Van Damme, Q. Hao, A. Barre, P. Rougé, F. Van Leuven, and W. J. Peumans
Major Protein of Resting Rhizomes of Calystegia sepium (Hedge Bindweed) Closely Resembles Plant RNases But Has No Enzymatic Activity
Plant Physiology, February 1, 2000; 122(2): 433 - 446.
[Abstract] [Full Text]

Home page
 Plant CellHome page
D. P. Matton, D. T. Luu, Q. Xike, G. Laublin, M. O'Brien, O. Maes, D. Morse, and M. Cappadocia
Production of an S RNase with Dual Specificity Suggests a Novel Hypothesis for the Generation of New S Alleles
PLANT CELL, November 1, 1999; 11(11): 2087 - 2098.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1998 by the American Society of Plant Biologists