EVALUATION OF DESICCANTS Z ITE BEADS TECHNOLOGY FOR DRYING FOUR SEED CROPS (GREEN GRAM-VIGNA RADIATA L., ONION-ALLIUM CEPA L., AMARANTHUS L., TOMATO- LYCOPERSCON ESCULENTUM L.) AND THEIR EFFECT ON SEED STORABILITY AND QUALITY

The Physiological quality of the seed is challenged by processing and handling methods especially drying methods, packaging materials, storage method used and time. A comparable study was conducted to evaluate influences of different seeds’ drying methods, packaging materials and storage period on tomato, green gram, onion and amaranth. A Randomized complete Block Design (RCBD) factorial experiment with four factors (crop types, seed storage period, packaging materials and drying methods (4 x 4 x 2 x 2) resulted in a combination of 32 treatments used. Results revealed that there was highly significant difference (P<.001) among treatments over seed qualities. It was observed that seeds dried with zeolite beads and stored with air tight container had good seed quality over seeds dried under sun and stored with cloth bag. Seed dried using zeolite beads and stored with airtight container except amaranth showed higher germination percentage (green gram 74), (onion 87) and (tomato, 80), field emergence percentage (green gram 70), (onion 83) and (tomato 79) and vigour index I (green gram 1070), (onion 987) and (tomato, 1122) compared to germination percentage of sundried seeds stored with cloth bag (green gram 18), (onion 64), (tomato, 60), field emergence percentage (green gram 15), (onion 61), (tomato, 58) and vigour Index I (green gram 226), (onion 653), (tomato, 768) after 18 months of storage

The FUS gene is dual-coding with both proteins contributing to FUS-mediated toxicity

Novel functional coding sequences (altORFs) are camouflaged within annotated ones (CDS) in a different reading frame. We show here that an altORF is nested in the FUS CDS, encoding a conserved 170 amino acid protein, altFUS. AltFUS is endogenously expressed in human tissues, notably in the motor cortex and motor neurons. Over-expression of wild-type FUS and/or amyotrophic lateral sclerosis-linked FUS mutants is known to trigger toxic mechanisms in different models. These include inhibition of autophagy, loss of mitochondrial potential and accumulation of cytoplasmic aggregates. We find that altFUS, not FUS, is responsible for the inhibition of autophagy, and pivotal in mitochondrial potential loss and accumulation of cytoplasmic aggregates. Suppression of altFUS expression in a Drosophila model of FUS-related toxicity protects against neurodegeneration. Some mutations found in ALS patients are overlooked because of their synonymous effect on the FUS protein. Yet, we show they exert a deleterious effect causing missense mutations in the overlapping altFUS protein. These findings demonstrate that FUS is a bicistronic gene and suggests that both proteins, FUS and altFUS, cooperate in toxic mechanisms