Plant Glutathione Transferases: Structure, Antioxidant Catalytic Function and in planta Protective Role in Biotic and Abiotic Stress

Plant cytosolic glutathione transferases (GSTs) belong to an ancient enzyme superfamily with multiple and diverse functions which are important in counteracting biotic and abiotic stress. GSTs catalyze the conjugation of xenobiotics and endogenous electrophilic compounds with glutathione (GSH), leading to their detoxification. GSTs not only catalyze detoxification reactions but they are also involved in GSH-dependent isomerization reactions, in GSH-dependent reduction of organic hydroperoxides, biosynthesis of secondary metabolites, and exhibit thioltransferase and dehydroascorbate reductase activity. The applications of ‘omics’ technologies have allowed the classification of GSTs and the study of their evolution and sequence diversity, while enzymology has provided powerful insights into their catalytic role. This review focuses on plant GSTs, and attempts to give an overview of the new insights into their catalytic function and biological role in biotic and abiotic stress tolerance mechanisms in plants

Sequence-related amplified polymorphism (SRAP) markers, an efficient and affordable tool for evaluation genetic diversity in forest areas

This article describes testing the application of SRAP (sequence-related amplified polymorphism) markers for characterisation of a small set of plants of Quercus coccifera L and samples from 25 other forest tree species. The results suggest that SRAP markers could be used as an affordable and efficient tool for the characterisation of the genetic diversity in populations of tree species as a part of the characterisation of forest biodiversity and the related decision making and management