Identification of stylar RNases associated with gametophytic self-incompatibility in almond (Prunus dulcis)

• Published in: Plant and cell physiology 1997-03, Vol.38 (3), p.304-311
• Main Authors: Tao, R. (Kyoto Univ. (Japan). Coll. of Agriculture), Yamane, H, Sassa, H, Mori, H, Gradziel, T.M, Dandekar, A.M, Sugiura, A
• Format: Article
• Language: English
• Subjects: Agronomy. Soil science and plant productions; Almond; Amino Acid Sequence; AUTOESTERILIDAD; AUTOSTERILITE; Biological and medical sciences; DETERIORATION; DETERIORO; Fundamental and applied biological sciences. Psychology; GAMETE; GAMETES; GAMETOS; Gasmetophytic self incompatibitity; Genetics and breeding of economic plants; Genotype; GINECEO; Glycoproteins - analysis; GYNECEE; GYNOECIUM; Heterosis. Floral biology applications: apomixy, male sterility, incompatibility, varia; IDENTIFICACION; IDENTIFICATION; ISoelectric focusing; Molecular Sequence Data; Nuts - enzymology; Nuts - genetics; Peptide Fragments; Plant breeding: fundamental aspects and methodology; Plant physiology and development; Plant Proteins - analysis; Plant Proteins - chemistry; PRUNUS AMYGDALUS; Prunus dulcis; RIBONUCLEASAS; RIBONUCLEASE; RIBONUCLEASES; Ribonucleases - analysis; Ribonucleases - chemistry; S-RNase; SELF STERILITY; Sequence Homology, Amino Acid; Sexual reproduction; Two dimensional gel electrophoresis; Vegetative and sexual reproduction, floral biology, fructification
• ISSN: 0032-0781; 1471-9053
• DOI: 10.1093/oxfordjournals.pcp.a029167

Stylar proteins of 13 almond (Prunus dulcia) cultivars with known S-genotypes were surveyed by IEF and 2D-PAGE combined with immunoblot and N-terminal amino acid sequence analyses to identify S-RNase associated with gametophytic self-incompatibility (SI) in this plant species. RNase activities corresponding to Sa and Sb two of the four S-alleles tested, were identified by IEF and RNase activity staining. The Sa-RNase band reacted with the anti-S4-serum prepared from Japanese pear (Pyrus serotina); no reaction with the anitserum was observed with the Sb-RNase band. When the Sa-RNase band was excised from an IEF gel stained for RNase activity, subjected to SDS-PAGE, and detected by immunoblotting, it appeared that this band consisted of a single protein that reacted with the anti-S4-serum with Mr of about 28 kDa. With 2D-PAGE and silver staining of the stylar extracts, all four S-proteins could be successfully distinguished from each other in the highly basic zone of the gel