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The authors show that the Salmonella effector SopF is activated by ARF GTPases to ADP-ribosylate a glutamine in the V-ATPase subunit ATP6V0C, blocking xenophagy or other selective autophagy types independent of proton-pumping activity.
An elegant cryo-EM and biophysical study unveils the conformational changes of the E. coli MutS mismatch repair factor. This provides a nice follow-up to the recent report from the same group characterizing how MutS scans DNA without initiating repair on correctly base-paired DNA and recruits MutL upon encountering a mismatch.
Retinal photoreceptor cyclic nucleotide-gated (CNG) ion channels convert light signals to electrical signals in the eye. Their structures have been solved at ~3 Å resolution by cryo-EM; the asymmetric subunit assembly of heteromeric CNG channels produces a unique ion-permeation pathway with an unusual gating apparatus that indicates distinct subunit contributions for ligand-dependent channel activation.
Cryogenic electron microscopy structures of Escherichia coli MutS at sequential stages of the ATP hydrolysis cycle reveal how ATP binding and hydrolysis and its modulation by DNA enable MutS to adopt different conformations during mismatch repair.
A series of cryo-EM structures of human IMPDH1 variants reveal polymorphic filaments. Blindness-associated mutations in IMPDH1 are characterized and half disrupt feedback inhibition. Together, these findings are a foundation for understanding IMPDH1 in retinal function and disease.
New data reveal a sequential mode of alternative polyadenylation. Distal polyA sites are processed first and the resultant transcripts are retained in the nuclear-chromatin matrix for subsequent cleavage and polyadenylation at proximal polyA sites.