RDE-1 slicer activity is required only for passenger-strand cleavage during RNAi in Caenorhabditis elegans.

TY - JOUR

T1 - RDE-1 slicer activity is required only for passenger-strand cleavage during RNAi in Caenorhabditis elegans.

AU - Steiner, F.A.

AU - Okihara, K.L.

AU - Hoogstrate, S.W.

AU - Sijen, T.

AU - Ketting, R.F.

N1 - Reporting year: 2009

PY - 2009

Y1 - 2009

N2 - RNA interference (RNAi) is a process in which double-stranded RNA is cleaved into small interfering RNAs (siRNAs) that induce the destruction of homologous single-stranded mRNAs. Argonaute proteins are essential components of this silencing process; they bind siRNAs directly and can cleave RNA targets using a conserved RNase H motif. In Caenorhabditis elegans, the Argonaute protein RDE-1 has a central role in RNAi. In animals lacking RDE-1, the introduction of double-stranded RNA does not trigger any detectable level of RNAi. Here we show that RNase H activity of RDE-1 is required only for efficient removal of the passenger strand of the siRNA duplex and not for triggering the silencing response at the target-mRNA level. These results uncouple the role of the RDE-1 RNase H activity in small RNA maturation from its role in target-mRNA silencing in vivo.

AB - RNA interference (RNAi) is a process in which double-stranded RNA is cleaved into small interfering RNAs (siRNAs) that induce the destruction of homologous single-stranded mRNAs. Argonaute proteins are essential components of this silencing process; they bind siRNAs directly and can cleave RNA targets using a conserved RNase H motif. In Caenorhabditis elegans, the Argonaute protein RDE-1 has a central role in RNAi. In animals lacking RDE-1, the introduction of double-stranded RNA does not trigger any detectable level of RNAi. Here we show that RNase H activity of RDE-1 is required only for efficient removal of the passenger strand of the siRNA duplex and not for triggering the silencing response at the target-mRNA level. These results uncouple the role of the RDE-1 RNase H activity in small RNA maturation from its role in target-mRNA silencing in vivo.

U2 - 10.1038/nsmb.1541

DO - 10.1038/nsmb.1541

M3 - Article

SN - 1545-9985

VL - 16

SP - 207

EP - 211

JO - Nature Structural & Molecular Biology

JF - Nature Structural & Molecular Biology

IS - 2

ER -