Abstract:
:HEPN (Higher Eukaryotes and Prokaryotes Nucleotide-binding) RNases are an emerging class of functionally diverse RNA processing and degradation enzymes. Members are defined by a small α-helical bundle encompassing a short consensus RNase motif. HEPN dimerization is a universal requirement for RNase activation as the conserved RNase motifs are precisely positioned at the dimer interface to form a composite catalytic center. While the core HEPN fold is conserved, the organization surrounding the HEPN dimer can support large structural deviations that contribute to their specialized functions. HEPN RNases are conserved throughout evolution and include bacterial HEPN RNases such as CRISPR-Cas and toxin-antitoxin associated nucleases, as well as eukaryotic HEPN RNases that adopt large multi-component machines. Here we summarize the canonical elements of the growing HEPN RNase family and identify molecular features that influence RNase function and regulation. We explore similarities and differences between members of the HEPN RNase family and describe the current mechanisms for HEPN RNase activation and inhibition.
journal_name
Crit Rev Biochem Mol Bioljournal_title
Critical reviews in biochemistry and molecular biologyauthors
Pillon MC,Gordon J,Frazier MN,Stanley REdoi
10.1080/10409238.2020.1856769subject
Has Abstractpub_date
2021-02-01 00:00:00pages
88-108issue
1eissn
1040-9238issn
1549-7798journal_volume
56pub_type
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