RNase HII from Chlamydia pneumoniae discriminates mismatches incorporation into DNA-rN1-DNA/DNA duplexes.
It was reported that RNase HII from Chlamydia pneumoniae (CpRNase HII) had RNase H activity on RNA/DNA duplex. We have analyzed the cleavage specificity of CpRNase HII on DNA-rN1-DNA/DNA duplex (rN1, one ribonucleotide). Various mismatches were introduced into the DNA-rN1-DNA/DNA duplexes at or around the ribonucleotide. The mismatches of duplexes resulted in slower cleavage rates compared to the matched duplexes. Furthermore, a greater reduction in cleavage activity was observed for the mismatches located at or adjacent to the ribonucleotide. The mismatches at the same position of DNA-rN1-DNA/DNA duplexes have different impact on the cleavage rates of CpRNase HII depending on the types of mismatches. These findings may offer further insights into the physical binding and catalytic properties of CpRNase HII-substrate interaction.
Hou
Jingli
J
College of Life Science & Technology, Shanghai Jiaotong University, 800 Dong-Chuan Road, Shanghai 200240, China.
Liu
Xipeng
X
Pei
Dongli
D
Liu
Jianhua
J
D020137:Base Pair Mismatch; D001665:Binding Sites; D002384:Catalysis; D016993:Chlamydophila pneumoniae / Q000201:enzymology*; D004247:DNA / Q000737:chemistry* / Q000378:metabolism*; D004789:Enzyme Activation; D011485:Protein Binding; D016914:Ribonuclease H / Q000737:chemistry* / Q000378:metabolism*
D004247:DNA; C091139:ribonuclease HII; D016914:Ribonuclease H