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Self-compatibility in aLycopersicon peruvianum variant (LA2157) is associated with a lack of style S-RNase activity
Authors:Y. Kowyama  C. Kunz  I. Lewis  E. Newbigin  A. E. Clarke  M. A. Anderson
Affiliation:(1) Plant Cell Biology Research Centre, School of Botany, University of Melbourne, 3052 Parkville, Victoria, Australia;(2) Present address: Faculty of Bioresources, Mie University, 514 Tsu, Japan
Abstract:A series of crosses between a naturally-occurring self-compatible accession ofLycopersicon peruvianum and a closely-related self-incompatible accession were used to demonstrate that the mutation to self-compatibility is located at the S-locus. Progeny of the crosses contain abundant style proteins of about 30 kDa that segregate with the S6and S7-alleles from the SI parent and the Sc-allele from the SC parent. The S6and S7-associated proteins have ribonuclease activity whereas the Sc-associated protein is not an active ribonuclease. This finding indicates that S-RNases are determinants of self-incompatibility in the style and that the ribonuclease activity is essential for their function.
Keywords:Tomato  Lycopersicon peruvianum  Self-incompatibility  S-locus mutation  Pollination Style-ribonuclease (S-RNase)
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