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HnRNPA1 Specifically Recognizes the Base of Nucleotide at the Loop of RNA G-Quadruplex.

ABSTRACT: Human telomere RNA performs various cellular functions, such as telomere length regulation, heterochromatin formation, and end protection. We recently demonstrated that the loops in the RNA G-quadruplex are important in the interaction of telomere RNA with heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1). Here, we report on a detailed analysis of hnRNPA1 binding to telomere RNA G-quadruplexes with a group of loop variants using an electrophoretic mobility shift assay (EMSA) and circular dichroism (CD) spectroscopy. We found that the hnRNPA1 binds to RNA G-quadruplexes with the 2'-O-methyl and DNA loops, but fails to bind with the abasic RNA and DNA loops. These results suggested that hnRNPA1 binds to the loop of the RNA G-quadruplex by recognizing the base of the loop's nucleotides. The observation provides the first evidence that the base of the loop's nucleotides is a key factor for hnRNPA1 specifically recognizing the RNA G-quadruplex.

SUBMITTER: Liu X

PROVIDER: S-EPMC6017123 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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HnRNPA1 Specifically Recognizes the Base of Nucleotide at the Loop of RNA G-Quadruplex.

Liu Xiao X Xu Yan Y

Molecules (Basel, Switzerland) 20180122 1

Human telomere RNA performs various cellular functions, such as telomere length regulation, heterochromatin formation, and end protection. We recently demonstrated that the loops in the RNA G-quadruplex are important in the interaction of telomere RNA with heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1). Here, we report on a detailed analysis of hnRNPA1 binding to telomere RNA G-quadruplexes with a group of loop variants using an electrophoretic mobility shift assay (EMSA) and circular dich ...[more]

PMID: 29361764

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