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The human ribosomal protein S3 (rpS3) functions as a component of the 40S subunit and as a UV DNA repair endonuclease. This enzyme has an endonuclease activ- ity for UV-irradiated and oxidatively damaged DNAs. DNA repair endonucleases recognize a variety of UV and oxidative base damages in DNA from E. coli to human cells. E. coli endonuclease III is especially known to have an iron-sulfur cluster as a co-factor. Here, we tried an electron paramagnetic resonance (EPR) method for the first time to observe a known iron-sulfur cluster signal from E. coli endonuclease III that was previously reported. We compared it to the human rpS3 in order to find out whether or not the human protein contains an iron-sulfur cluster. As a result, we succeeded in observing a Fe EPR signal that is apparently from an iron-sulfur cluster in the human rpS3 endonuclease. The EPR signal from the human enzyme, consisting of three major parts, is similar to that from the E. coli enzyme, but it has a distinct extra peak.


The human ribosomal protein S3 (rpS3) functions as a component of the 40S subunit and as a UV DNA repair endonuclease. This enzyme has an endonuclease activity for UV-irradiated and oxidatively damaged DNAs. DNA repair endonucleases recognize a variety of UV and oxidative base damages in DNA from E. coli to human cells. E. coli endonuclease III is especially known to have an iron-sulfur cluster as a co-factor. Here, we tried an electron paramagnetic resonance (EPR) method for the first time to observe a known iron-sulfur cluster signal from E. coli endonuclease III that was previously reported. We compared it to the human rpS3 in order to find out whether or not the human protein contains an iron-sulfur cluster. As a result, we succeeded in observing a Fe EPR signal that is apparently from an iron-sulfur cluster in the human rpS3 endonuclease. The EPR signal from the human enzyme, consisting of three major parts, is similar to that from the E. coli enzyme, but it has a distinct extra peak.