Abstract
The interaction between ribosome-inactivating proteins (RIPs) and supercoiled DNA was observed with an atomic force microscope (AFM). It was found that RIPS can bind to both supercoiled DNA and the unwound double-stranded loop region in supercoiled DNA. The RIPS bound to the supercoils can induce the conformational change of supercoiled DNA. Furthermore, the supercoiled DNA was relaxed and cleaved into nick or linear form by RIPs. It indicated that RIP seemed to be a supercoil-dependent DNA binding protein and exhibited the activity of supercoil-dependent DNA endonuclease.
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