Structural and biophysical insights into the unique RNase YicC
- 1Icahn School of Medicine at Mount Sinai
Abstract
RNA cleavage and processing are highly conserved regulatory mechanisms across bacteria. We recently discovered a novel family of RNases called YicC, conserved across all bacteria but unrelated to known RNase families. The cryo-EM structure of RNA bound to Escherichia coli YicC endonuclease suggested a clamshell-like ribonuclease mechanism for cleavage, although its exact mechanism and function remain elusive. Here, we report new cryo-EM structures that provide snapshots of the closing of the complex and also capture a surprising dimeric-RNA:protein complex. We further characterize the RNA cleavage targets in solution using nuclear magnetic resonance (NMR) spectroscopy, and use all-atom molecular dynamics (MD) simulations to study Mg2+ binding. Our findings suggest that the YicC family can bind RNA hairpin structures and dimeric conformations with appropriate sequence and structural constraints, with cleavage driven strongly by Mg2+ ion localization. This study therefore provides overall insight into the novel cleavage mechanism of the highly conserved family of YicC-like endoribonucleases.
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BibTeX
@misc{wu2026structural,
title = {{Structural and biophysical insights into the unique RNase YicC}},
author = {R. Wu and H. Venkatesh and C. Lansiquot and S. A. Barnes and A. Golestanian and O. Rechkoblit and A. N. Jones and D. H. Bechhofer and M. B. Lazarus},
howpublished = {bioRxiv},
year = {2026},
month = sep,
doi = {10.64898/2026.09.15.751841},
url = {https://www.biorxiv.org/content/10.64898/2026.09.15.751841v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - Structural and biophysical insights into the unique RNase YicC
AU - R. Wu
AU - H. Venkatesh
AU - C. Lansiquot
AU - S. A. Barnes
AU - A. Golestanian
AU - O. Rechkoblit
AU - A. N. Jones
AU - D. H. Bechhofer
AU - M. B. Lazarus
PY - 2026
DA - 2026/09/15
PB - bioRxiv
DO - 10.64898/2026.09.15.751841
UR - https://www.biorxiv.org/content/10.64898/2026.09.15.751841v1
AB - RNA cleavage and processing are highly conserved regulatory mechanisms across bacteria. We recently discovered a novel family of RNases called YicC, conserved across all bacteria but unrelated to known RNase families. The cryo-EM structure of RNA bound to Escherichia coli YicC endonuclease suggested a clamshell-like ribonuclease mechanism for cleavage, although its exact mechanism and function remain elusive. Here, we report new cryo-EM structures that provide snapshots of the closing of the complex and also capture a surprising dimeric-RNA:protein complex. We further characterize the RNA cleavage targets in solution using nuclear magnetic resonance (NMR) spectroscopy, and use all-atom molecular dynamics (MD) simulations to study Mg2+ binding. Our findings suggest that the YicC family can bind RNA hairpin structures and dimeric conformations with appropriate sequence and structural constraints, with cleavage driven strongly by Mg2+ ion localization. This study therefore provides overall insight into the novel cleavage mechanism of the highly conserved family of YicC-like endoribonucleases.
ER -