Publications by authors named "Heather R Dahlin"
Structural insights into RNA cleavage by a novel family of bacterial RNases.
Nucleic Acids Res
September 2024
Article Synopsis
- The study focuses on Escherichia coli's YicC protein, a newly identified ribonuclease crucial for RNA processing in living organisms.
- Researchers have characterized the structure of YicC in two forms: an unbound state (apo) and one bound to RNA, revealing unique structural features like a clamshell shape that are different from known ribonucleases.
- Findings highlight the importance of a specific domain (DUF1732) in RNA binding and catalytic activity, providing new insights into the functions of the YicC RNase family.
Protein-interaction domains can create unique macromolecular complexes that drive evolutionary innovation. By combining bioinformatic and phylogenetic analyses with structural approaches, we have discovered that the docking and dimerization (D/D) domain of the PKA regulatory subunit is an ancient and conserved protein fold. An archetypal function of this module is to interact with A-kinase-anchoring proteins (AKAPs) that facilitate compartmentalization of this key cell-signaling enzyme.
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