Sandbox 1: Difference between revisions

Recently, the discovery of other binding substrates with Hfq has expanded the regulatory spectrum of this protein. It was found that this RNA chaperone can also bind with rRNA, tRNA, and DNA. Studies have shown that Hfq promotes ribosome assembly in bacteria, where this protein is required for the processing of pre-16S and folding of the mature 16S rRNA in E. coli, displaying Hfq as an important ribosome biogenesis factor in bacterias. This process seems to be independent of Hfq interactions with sRNAs, which the binding surfaces of the vast majority of the Hfq-dependent sRNAs are the proximal and rim faces, and for the rRNA, in the distal face of the Hfq. The same was observed for tRNA, where Hfq was also associated as an important pre-tRNA maturation factor, however, the binding of the structural elements of tRNAs occurs through the proximal face of Hfq.

Notably, the regulatory activity of Hfq is not restricted to RNAs, it was also found to bind DNA, acting as an important factor in chromosome structure. Hfq was found to form a fiber like structure that leads, indirectly, to chromosome compaction through a mechanism still elusive. It is also associated with the regulation of cellular replication and transfer of several transposon systems (Santos et al., 2019).