Cloning and sequencing of cDNAs encoding two S proteins of a self-compatible cultivar of Petunia hybrida.
A defective S-allele, S(o), and a functional S-allele, Sx, have previously been found to be retained in an F1 hybrid of a self-compatible commercial cultivar of Petunia hybrida. Pistil proteins associated with these two alleles have also been identified. Their amino-terminal sequences have been found to share a high degree of similarity with those of S-proteins characterized from self-incompatible solanaceous species. Here we report the isolation and sequencing of cDNAs encoding S(o)- and Sx-proteins. Their deduced amino acid sequences contain all the consensus primary structural features of S-proteins from self-incompatible solanaceous species. Both proteins also have ribonuclease activity. The implications of these findings are discussed in relation to the presumed function of the S-protein in the self-incompatibility interaction.
Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.
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D000483:Alleles; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003433:Crosses, Genetic; D004247:DNA / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D018521:Plant Physiological Phenomena; D010940:Plant Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D010944:Plants / Q000235:genetics*; D012260:Ribonucleases / Q000235:genetics / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid
D010940:Plant Proteins; C075588:S-allele-associated protein Sx, Petunia hybrida; C075589:S-allele-associated protein So, Petunia hybrida; D004247:DNA; D012260:Ribonucleases