AI 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.
Article Abstract
Processing of RNA is a key regulatory mechanism for all living systems. Escherichia coli protein YicC belongs to the well-conserved YicC family and has been identified as a novel ribonuclease. Here, we report a 2.8-Å-resolution crystal structure of the E. coli YicC apo protein and a 3.2-Å-cryo-EM structure of YicC bound to an RNA substrate. The apo YicC forms a dimer of trimers with a large open channel. In the RNA-bound form, the top trimer of YicC rotates nearly 70° and closes the RNA substrate inside the cavity to form a clamshell-pearl conformation that resembles no other known RNases. The structural information combined with mass spectrometry and biochemical data identified cleavage on the upstream side of an RNA hairpin. Mutagenesis studies demonstrated that the previously uncharacterized domain, DUF1732, is critical in both RNA binding and catalysis. These studies shed light on the mechanism of the previously unexplored YicC RNase family.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11417398 | PMC |
| http://dx.doi.org/10.1093/nar/gkae717 | DOI Listing |
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