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Biology subjects

Aaquib, M.

Publications and source records attributed to Aaquib, M..

2 recordsLinked to original sources

Phosphorylation of Z granule components regulates germ granule organization and RNAi inheritance

Small RNAs represent important carriers of epigenetic information in nematodes, and factors involved in their biogenesis reside within perinuclear germ granules. Among these condensates, Z granules are essential for the inheritance of RNA interference (RNAi). The mechanisms by which Z granules form and promote this process remain unclear. We show that Casein kinase I alpha (KIN-19) is present in Z granules and associated with DEPS-1 and HERD-1 phosphorylation. In the absence of DEPS-1 and HERD-1 phosphorylation, animals have enlarged Z granules and enhanced RNAi inheritance. We propose that DEPS-1 acts as a phosphorylation-regulated scaffold that bridges ZNFX-1 and HERD-1 proteins. Our study demonstrates that Casein kinase I alpha-mediated phosphorylation is an important factor in germ granule modulation and RNAi inheritance, and additionally provides a novel molecular scaffold for understanding germ granule complexity in C. elegans.

molecular biology↗

Dicarboxylic acids synergize with yeast and human Hsp60/10 systems to mimic GroEL/ES

GroEL/ES has been the archetype to understand the function of the class I chaperonins (Hsp60/10 systems). While very similar in structure, the human or yeast mitochondrial one has diminished negative charge density in the central cavity. These chaperones had also lost their ability to assist a substrate of E.coli GroEL/ES. Here, we show that the eukaryotic Hsp60/10 systems can synergize with dicarboxylic acids in vitro at the physiological concentration of these metabolites to mimic the activity of E. coli GroEL/ES. Combining these Hsp60/10s and metabolites effectively alters the folding landscape like GroEL/ES; this is specific for the eukaryotic chaperonins and not the prokaryotic homologs with less negatively charged cavities. Thus, we identify a potential cooperation between molecular and chemical chaperones that may have important physiological implications linking metabolism to proteostasis.

biophysics↗