Identification of an intracellular pyrimidine-specific endoribonuclease from Bacillus subtilis.
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.
Mathur
S
S
Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Cannistraro
V J
VJ
Kennell
D
D
D001412:Bacillus subtilis / Q000201:enzymology*; D004722:Endoribonucleases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D013379:Substrate Specificity
D004722:Endoribonucleases; C029493:ribonuclease C