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GrainGenes Reference Report: PMP-58-183

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Reference	PMP-58-183
Title	Drechslera teres-infected barley (Hordeum vulgare L.) leaves accumulate eight isoforms of thaumatin-like proteins
Journal	Physiological and Molecular Plant Pathology
Year	2001
Volume	58
Pages	183-188
Author	Reiss E Horstmann C
Abstract	Summary: 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
Keyword	[ Hide all but 1 of 39 ] acid adaptation amino acid amino acid sequence barley basic proteins cdna cdna clone cdna sequence cdna sequence analysis chain chitinase clone defense drechslera teres electrophoresis full-length cdna hordeum hordeum vulgare isoform isolation n-terminal sequencing osmotin pathogenesis-related protein pcr peptide plant science polymerase polymerase chain reaction pr-5 protein protein residue sequence sequence data signal signal peptide site thaumatin-like protein two-dimensional electrophoresis

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