期刊
ACS OMEGA
卷 5, 期 10, 页码 5202-5208出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsomega.9b04221
关键词
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资金
- JGC-S Scholarship Foundation [17K05930]
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
G-quadruplexes have important biologic functions that are regulated by G-quadruplex-binding proteins. In particular, G-quadruplex structures are folded or unfolded by their binding proteins and affect transcription and other biologic functions. Here, we investigated the effect of the RNA recognition motif (RRM) and arginine-glycine-glycine repeat (RGG) domain of nucleolin on G-quadruplex formation. Our findings indicate that Phe in the RGG domain of nucleolin is responsible for G-quadruplex binding and folding. Moreover, the RRM of nucleolin potentially binds to a guanine-rich single strand and folds the G-quadruplex with a 5'-terminal and 3'-terminal single strand containing guanine. Our findings contribute to our understanding of how the RRM and RGG domains contribute to G-quadruplex folding and unfolding.
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