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Poly-(ADP-ribosylation) is a post-translational modification with broad roles in cell signaling. A recently reported crystal structure reveals how the accessory factor HPF1 extends the catalytic active site of PARP1 and PARP2 to promote the specific ADP-ribosylation of serine residues, a prerequisite for dynamic chromatin changes induced by DNA damage.
Adenosine deaminases acting on RNA (ADARs) catalyze deamination of adenosine to inosine. irCLASH identifies dsRNA substrates of ADARs and defines new features of their RNA-binding and editing activity, improving our understanding of these enzymes and aiding with future therapeutic applications.
Recent studies report the first structures of two CALHM family members, describing unexpected oligomeric architecture and providing insights into the mechanism of function of CALHM channels.
Many AAA+ ATPases assemble as hexamers to unfold protein substrates using a hand-over-hand, threading mechanism, but the Bcs1 AAA+ ATPase facilitates mitochondrial membrane translocation of the folded iron–sulfur Rieske protein. Two reports reveal that Bcs1 adopts an unusual heptameric configuration and provide insights into a non-canonical translocation mechanism.
Technological advances have led to new insights into genome-wide arrangements of nucleosomes along the DNA and the folding of the chromosome fiber in nuclear space, revealing unexpected diversity.
