Drechslera teres-infected barley (Hordeum vulgare L.) leaves accumulate eight isoforms of thaumatin-like proteins

Eight thaumatin-like proteins of barley (Hordeum vulgare L.) (TLP1-TLP8) were detected in Drechslera teres infected leaves by two-dimensional electrophoresis followed by N-terminal microsequencing: four of them are acidic; four are basic proteins. Partial amino acid sequence data were used to generate polymerase chain reaction (PCR) clones employed for the isolation of four novel, nearly full-length cDNA sequences encoding TLP4, TLP6, TLP7, and TLP8. The cDNAs are characterized by sequence sites of very high GC content and they encode proteins with 171-233 amino acid residues. The N-termini of the deduced proteins were preceded by putative signal peptides of 22-25 amino acid residues. With a Clustal W based dendrogram similar sequences were assigned to those we obtained in this work. (C) 2001 Academic Press.