The Cbf5-Nop10 Complex is a Molecular Bracket that Organizes Box H/ACA RNPs

Journal Article · Thu Dec 01 04:00:00 EST 2005 · Nature Structural & Molecular Biology, 12(12):1101-1107

DOI:https://doi.org/10.1038/nsmb1036· OSTI ID:902045

Hamma, Tomoko; Reichow, Steve L; Varani, Gabriele; Ferre-D'Amare, Adrian R

Box H/ACA ribonucleoprotein particles (RNPs) catalyze RNA pseudouridylation and direct processing of ribosomal RNA, and are essential architectural components of vertebrate telomerases. H/ACA RNPs comprise four proteins and a multihelical RNA. Two proteins, Cbf5 and Nop10, suffice for basal enzymatic activity in an archaeal in vitro system. We now report their cocrystal structure at 1.95-A resolution. We find that archaeal Cbf5 can assemble with yeast Nop10 and with human telomerase RNA, consistent with the high sequence identity of the RNP componenets between archaea and eukarya. Thus, the Cbf5-Nop10 architecture is phylogenetically conserved. The structure shows how Nop10 buttresses the active site of Cbf5, and it reveals two basic troughs that bidirectionally extend the active site cleft. Mutagenesis results implicate an adjacent basic patch in RNA binding. This tripartite RNA-binding surface may function as a molecular bracket that organizes the multihelical H/ACA and telomerase RNAs.

• Research Organization: Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC05-76RL01830
• OSTI ID: 902045
• Journal Information: Nature Structural & Molecular Biology, 12(12):1101-1107, Journal Name: Nature Structural & Molecular Biology, 12(12):1101-1107 Journal Issue: 12 Vol. 12
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Environmental Molecular Sciences Laboratory
IN VITRO
MUTAGENESIS
PROCESSING
PROTEINS
RESOLUTION
RIBOSOMAL RNA
RNA
VERTEBRATES
YEASTS