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Y-Box-Binding Protein 1 Stimulates Abasic Site Cleavage
E E Alemasova1, K N Naumenko, N A Moor
1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, 630090, Russia. lavrik@niboch.nsc.ru.
Biochemistry. Biokhimiia
|March 1, 2018
Summary
Y-box-binding protein 1 (YB-1) affects DNA repair by interacting with AP endonuclease 1 (APE1). YB-1 stabilizes APE1 on double-stranded DNA, enhancing AP site cleavage, which is crucial for DNA repair and cancer treatment.
Area of Science:
- Molecular Biology
- DNA Repair Mechanisms
- Enzymology
Background:
- Apurinic/apyrimidinic (AP) sites are frequent DNA lesions critical in DNA repair.
- AP endonuclease 1 (APE1) is a key enzyme initiating AP site repair via magnesium-dependent hydrolysis.
- Elevated APE1 activity in cancer cells is linked to chemoresistance, making it a therapeutic target.
Purpose of the Study:
- To investigate the role of Y-box-binding protein 1 (YB-1) in the function of AP endonuclease 1 (APE1).
- To elucidate how YB-1 influences APE1 activity on different DNA substrates.
- To understand the impact of YB-1 on APE1's interaction with AP sites in DNA.
Main Methods:
- Biochemical assays to assess APE1 endonuclease activity.
- Analysis of APE1-DNA complex stabilization in the presence of YB-1.
- Enzyme kinetics studies under varying magnesium concentrations.
Main Results:
- YB-1 was found to stabilize the APE1 complex with double-stranded DNA containing AP sites.
- YB-1 stimulates APE1-catalyzed cleavage of AP sites, particularly at low magnesium concentrations.
- This contrasts with YB-1's previously observed inhibitory effect on AP site hydrolysis in single-stranded DNA.
Conclusions:
- YB-1 exhibits a dual role in modulating APE1 activity based on DNA substrate and magnesium concentration.
- YB-1's stabilization of APE1 on double-stranded DNA and stimulation of cleavage could have implications for DNA repair and cancer therapy.
- Further research is warranted to explore the therapeutic potential of targeting the YB-1/APE1 interaction in chemoresistant cancers.
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