The possible role of macroelement content on bud abscission in pistachio (Pistacia vera L.)

Pistachio is the economically important nut tree in Turkey. Alternate bearing is one of the most important problems in pistachio, and it has a negative effect on producers, consumers and the country's economy. The cultivar 'Uzun' is one of the most important commercial pistachio cultivars in Turkey, and it has strong tendency to alternate bearing. There are no nuts completely in "Off" year while the trees are highly productive in the following year ("ON" year). The physiological mechanisms of the bud abscission process caused alternate bearing is unknown. In this study it was aimed to detect a relation between nutrient uptake and alternate phenomena in the pistachio 'Uzun' cultivar. For this purpose, nutrition concentrations were determined in various physiological periods from full flowering to harvest in one year old shoots of 'Uzun' pistachio cultivar under arid conditions. The shoots were compared based on their N, P, K, Ca and Mg content on shoots of "ON" and "OFF" year trees separately. According to the results, N, P, K, Ca and Mg contents of shoots were changed in "ON" and "OFF" year shoot samples and varied during the developmental stage and generally N, Mg and Ca elements were detected higher in shoots of "ON" year trees, while P and K, higher in "OFF" year trees. © 2018 ISHS

A dystroglycan mutation associated with limb-girdle muscular dystrophy.

Dystroglycan, which serves as a major extracellular matrix receptor in muscle and the central nervous system, requires extensive O-glycosylation to function. We identified a dystroglycan missense mutation (Thr192→Met) in a woman with limb-girdle muscular dystrophy and cognitive impairment. A mouse model harboring this mutation recapitulates the immunohistochemical and neuromuscular abnormalities observed in the patient. In vitro and in vivo studies showed that the mutation impairs the receptor function of dystroglycan in skeletal muscle and brain by inhibiting the post-translational modification, mediated by the glycosyltransferase LARGE, of the phosphorylated O-mannosyl glycans on α-dystroglycan that is required for high-affinity binding to laminin