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Updated: Jul 25, 2026

Substrate Generation for Endonucleases of CRISPR/Cas Systems
Published on: September 9, 2012
Identification of an intracellular pyrimidine-specific endoribonuclease from Bacillus subtilis
S Mathur1, V J Cannistraro, D Kennell
1Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Abstract:
Two intracellular RNases which were easily separated by fractionation on strong anion- or cation-exchange resins were identified from Bacillus subtilis. One cleaved any phosphodiester bond, while the second cleaved only pyrimidine-N bonds. The enzyme with pyrimidine-N specificity was approximately 15 kDa, had a pH optimum of approximately 6.2, degraded C-C bonds approximately 10 times faster than U-U bonds, and was completely inactive against single-stranded DNA. The enzyme is called RNase C and may be the first reported broad-specificity endoribonuclease from B. subtilis.
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