TaSK5, an abiotic stress-inducible GSK3/shaggy-like kinase from wheat, confers salt and drought tolerance in transgenic Arabidopsis.

A novel cold-inducible GSK3/shaggy-like kinase, TaSK5, was isolated from winter wheat using a macroarray-based differential screening approach. TaSK5 showed high similarity to Arabidopsis subgroup I GSK3/shaggy-like kinases ASK-alpha, AtSK-gamma and ASK-epsilon. RNA gel blot analyses revealed TaSK5 induction by cold and NaCl treatments and to a lesser extent by drought treatment.

The expression of genes at locus is associated with the level of frost tolerance in Bulgarian winter wheat cultivars.

The regulation of the majority of cold-regulated genes in plants is mediated by () transcription factor family. Natural differences in frost tolerance (FT) of wheat have been mapped to the () locus on chromosome group 5 and are associated with variation in threshold induction temperatures and/or transcript levels of genes. This study used real-time reverse-transcription polymerase chain reaction (qRT-PCR) to compare the relative expression levels of four genes ( and ) in crown tissue of two Bulgarian hexaploid winter wheat cultivars (Milena and Russalka) with distinct levels of low-temperature (LT) tolerance but same vernalization requirement, and the spring cultivar Chinese Spring.

Identification of a novel LEA protein involved in freezing tolerance in wheat.

Late embryogenesis abundant (LEA) proteins are a family of hyper-hydrophilic proteins that accumulate in response to cellular dehydration. Originally identified as plant proteins associated with seed desiccation tolerance, LEA proteins have been identified in a wide range of organisms such as invertebrates and microorganisms. LEA proteins are thought to protect proteins and biomembranes under water-deficit conditions.

A cold inducible multidomain cystatin from winter wheat inhibits growth of the snow mold fungus, Microdochium nivale.

A novel cold-induced cystatin cDNA clone (TaMDC1) was isolated from cold acclimated winter wheat crown tissue by using a macroarray-based differential screening method. The deduced amino acid sequence consisted of a putative N-terminal secretory signal peptide of 37 amino acids and a mature protein (mTaMDC1) with a molecular mass of 23 kDa. The mTaMDC1 had a highly conserved N-terminal cystatin domain and a long C-terminal extension containing a second region, which exhibited partial similarity to the cystatin domain.