Characteristic of the gene candidate SecARS encoding alkylresorcinol synthase in Secale.

Background: Alkylresorcinols (ARs) are compounds belonging to the class of phenolic lipids. A rich source of ARs are cereal grains such as rye, wheat, triticale or barley. ARs found in plants are characterized by a variety of biological properties such as antimicrobial, antifungal and cytotoxic activity.

Calreticulin localizes to plant intra/extracellular peripheries of highly specialized cells involved in pollen-pistil interactions.

Calcium (Ca) plays essential roles in generative reproduction of angiosperms, but the sites and mechanisms of Ca storage and mobilization during pollen-pistil interactions have not been fully defined. Both external and internal Ca stores are likely important during male gametophyte communication with the sporophytic and gametophytic cells within the pistil. Given that calreticulin (CRT), a Ca-buffering protein, is able to bind Ca reversibly, it can serve as a mobile store of easily releasable Ca (so called an exchangeable Ca) in eukaryotic cells.

Proteinaceous toxins of Stagonospora nodorum, the causal agent of triticale leaf and glume blotch.

S. nodorum is an economically important necrotrophic pathogen of cereals and grasses worldwide. In past several years appeared in literature quite a number of reports on existence of proteinaceous effectors produced by the fungus which induce necrosis in cereal host tissue.

[Myosin VI: the unique motor protein of the actin cytoskeleton].

Myosins are actin-based motor proteins that use energy derived from ATP hydrolysis to generate force and move along actin filaments. Myosin VI is a unique motor protein because it moves towards the "minus" end of actin filament, which is the opposite direction to all of the other myosins studied so far, and therefore is thought to have unique properties and cellular functions. Localization and functional studies indicate that myosin VI plays a role in a variety of different intracellular processes, such as endocytosis and secretion as well as cell division, differentiation, and cell migration.

[Calreticulin--the structure, cell localizations and functions in animals and plants].

Calreticulin (CRT) is an ubiquitously expressed Ca2+ binding protein in endoplasmic reticulum (ER) of eukaryotic cells. A highly conserved structure between CRTs from different species of animals and plants confirms an important role of the protein in living cells. CRT has been found in different cellular compartments, suggesting to play a role in many cellular processes both inside and outside the ER.