Abstract
The expansion of CAG trinucleotide repeats has been considered to be highly related to the polyglutamine disorders which effect the neuron and muscle system of organism. This study aims to investigate how knocking down HSP90 or RPL36 would affect the polyglutamine toxicity. Based on the previous experiment, the Caenorhabditis elegans that expresses polyQ proteins would show protein misfolding and aggregation. We use C. elegans as model and record the phenotype of worms, frequency of thrashing and number of aggregations under IHA microscope before and after close the target genes by RNA interference. The results of this experiment indicate that HSP90 deficiency increases polyglutamine toxicity in muscle cells, presumably by preventing polyglutamine protein aggregation. Otherwise, rpl36 knockdown suppresses polyglutamine toxicity in muscle cells, perhaps by stimulating the aggregation of polyglutamine proteins. The research work has contributed to our present understanding to polyglutamine disorder and the possible function of HSP90 and RPL36.
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