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The study highlights the importance of water-mediated interactions in recognition of dinucleotides by transcription factors. Water’s influence on enthalpy and entropy modulates binding affinity and temperature sensitivity of TF binding.
A genetic variant specific to people of African ancestry increases the risk of neurodegenerative diseases, such as Parkinson disease (PD). This variant occurs in a noncoding region and interferes with the splicing of mRNA transcripts, resulting in lowered protein levels and activity. This work reveals a novel therapeutic target in an underserved and underrepresented population.
Bhatta et al. use biochemistry and cryogenic electron microscopy to elucidate the mechanism of human tRNA 3′ processing. Their results show how mitochondria-specific subunits of RNase Z compensate for the structural degeneracy of organellar tRNAs.
Here the authors show that codependence of dynein and kinesin KIF1C occurs through binding of the FTS–HOOK3–FHIP1B cargo adapter. Binding of KIF1C releases the HOOK3 autoinhibited folded conformation allowing dynein to bind the adapter. In this cocomplex, KIF1C further acts as a processivity factor for dynein.
