Journal Article

Molecular Characterization and Origin of Novel Bipartite Cold-regulated Ice Recrystallization Inhibition Proteins from Cereals

Karine Tremblay, François Ouellet, Julie Fournier, Jean Danyluk and Fathey Sarhan

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 46, issue 6, pages 884-891
Published in print June 2005 | ISSN: 0032-0781
Published online June 2005 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pci093
Molecular Characterization and Origin of Novel Bipartite Cold-regulated Ice Recrystallization Inhibition Proteins from Cereals

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To understand the molecular basis of freezing tolerance in plants, several low temperature-responsive genes have been identified from wheat. Among these are two genes named TaIRI-1 and TaIRI-2 (Triticum aestivum ice recrystallization inhibition) that are up-regulated during cold acclimation in freezing-tolerant species. Phytohormones involved in pathogen defense pathways (jasmonic acid and ethylene) induce the expression of one of the two genes. The encoded proteins are novel in that they have a bipartite structure that has never been reported for antifreeze proteins. Their N-terminal part shows similarity with the leucine-rich repeat-containing regions present in the receptor domain of receptor-like protein kinases, and their C-terminus is homologous to the ice-binding domain of some antifreeze proteins. The recombinant TaIRI-1 protein inhibits the growth of ice crystals, confirming its function as an ice recrystallization inhibition protein. The TaIRI genes were found only in the species belonging to the Pooideae subfamily of cereals. Comparative genomic analysis suggested that molecular evolutionary events took place in the genome of freezing-tolerant cereals to give rise to these genes with putative novel functions. These apparent adaptive DNA rearrangement events could be part of the molecular mechanisms that ensure the survival of hardy cereals in the harsh freezing environments.

Keywords: Antifreeze proteins; Freezing tolerance; Ice-binding proteins; Receptor-like kinase; Wheat; AFP, antifreeze protein; CA, cold acclimation; FT, freezing tolerance; IRI, ice recrystallization inhibition; JA, jasmonic acid; LRR, leucine-rich repeat; LT, low temperature; OsPR, Oryza sativa phytosulfokine receptor kinase; PR, pathogenesis-related; RI, recrystallization inhibition; RKD, receptor kinase domain; RLK, receptor-like kinase; RLP, receptor-like protein; SA, salicylic acid; TE, transposable element; TH, thermal hysteresis

Journal Article.  5626 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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