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Title: RNA triplexes : from structural principles to biological and biotech applications
Authors: Devi, Gitali
Zhou, Yuan
Zhong, Zhensheng
Toh, Desiree-Faye Kaixin
Chen, Gang
Keywords: DRNTU::Science::Chemistry::Biochemistry
Issue Date: 2014
Source: Devi, G., Zhou, Y., Zhong, Z., Toh, D.-F. K., & Chen, G. (2015). RNA triplexes: from structural principles to biological and biotech applications. Wiley interdisciplinary reviews : RNA, 6(1), 111-128.
Series/Report no.: Wiley interdisciplinary reviews : RNA
Abstract: The diverse biological functions of RNA are determined by the complex structures of RNA stabilized by both secondary and tertiary interactions. An RNA triplex is an important tertiary structure motif that is found in many pseudoknots and other structured RNAs. A triplex structure usually forms through tertiary interactions in the major or minor groove of a Watson–Crick base-paired stem. A major-groove RNA triplex structure is stable in isolation by forming consecutive major-groove base triples such as U·A-U and C+·G-C. Minor-groove RNA triplexes, e.g., A-minor motif triplexes, are found in almost all large structured RNAs. As double-stranded RNA stem regions are often involved in biologically important tertiary triplex structure formation and protein binding, the ability to sequence specifically target any desired RNA duplexes by triplex formation would have great potential for biomedical applications. Programmable chemically modified triplex-forming oligonucleotides (TFOs) and triplex-forming peptide nucleic acids (PNAs) have been developed to form TFO·RNA2 and PNA·RNA2 triplexes, respectively, with enhanced binding affinity and sequence specificity at physiological conditions. Here, we (1) provide an overview of naturally occurring RNA triplexes, (2) summarize the experimental methods for studying triplexes, and (3) review the development of TFOs and triplex-forming PNAs for targeting an HIV-1 ribosomal frameshift-inducing RNA, a bacterial ribosomal A-site RNA, and a human microRNA hairpin precursor, and for inhibiting the RNA–protein interactions involving human RNA-dependent protein kinase and HIV-1 viral protein Rev. WIREs RNA 2015, 6:111–128. doi: 10.1002/wrna.1261
ISSN: 1757-7004
DOI: 10.1002/wrna.1261
Schools: School of Physical and Mathematical Sciences 
Rights: © 2014 John Wiley & Sons, Ltd. This is the author created version of a work that has been peer reviewed and accepted for publication by Wiley Interdisciplinary Reviews: RNA, John Wiley & Sons, Ltd. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

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