Human Argonaute 2 Has Diverse Reaction Pathways on Target RNAs

Myung Hyun Jo, Soochul Shin, Seung Ryoung Jung, Eunji Kim, Ji Joon Song, Sungchul Hohng

Research output: Contribution to journalArticlepeer-review


Argonaute is a key enzyme of various RNA silencing pathways. We use single-molecule fluorescence measurements to characterize the reaction mechanisms of the core-RISC (RNA-induced silencing complex) composed of human Argonaute 2 and a small RNA. We found that target binding of core-RISC starts at the seed region, resulting in four distinct reaction pathways: target cleavage, transient binding, stable binding, and Argonaute unloading. The target cleavage requires extensive sequence complementarity and dramatically accelerates core-RISC recycling. The stable binding of core-RISC is efficiently established with the seed match only, providing a potential explanation for the seed-match rule of miRNA (microRNA) target selection. Target cleavage on perfect-match targets sensitively depends on RNA sequences, providing an insight into designing more efficient siRNAs (small interfering RNAs).

Original languageEnglish (US)
Pages (from-to)117-124
Number of pages8
JournalMolecular cell
Issue number1
StatePublished - 2015
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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