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The Spliceosome: Design Principles of a Dynamic RNP Machine
The spliceosome exhibits exceptional compositional and structural dynamics that are exploited during substrate-dependent complex assembly, catalytic activation, and active site remodeling in the pre-mRNAs. Expand
Single-Stranded Antisense siRNAs Guide Target RNA Cleavage in RNAi
- Javier Martinez, A. Patkaniowska, H. Urlaub, R. Lührmann, T. Tuschl
- Biology, Medicine
- 6 September 2002
A human biochemical system that recapitulates siRNA-mediated target RNA degradation by using affinity-tagged siRNAs is described and it is demonstrated that a single-stranded siRNA resides in the RNA-induced silencing complex (RISC) together with eif2C1 and/or eIF2C2 (human GERp95) Argonaute proteins. Expand
Spliceosome structure and function.
The extensive interplay of RNA and proteins in aligning the pre-mRNA's reactive groups, and the presence of both RNA and protein at the core of the splicing machinery, suggest that the spliceosome is an RNP enzyme, but elucidation of the precise nature of its active site awaits the generation of a high-resolution structure of its RNP core. Expand
The HIV-1 Rev Activation Domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
The Rev activation domain constitutes a nuclear export signal that redirects RRE-containing viral RNAs to a non-mRNA export pathway. Expand
Identification of Novel Argonaute-Associated Proteins
The authors' biochemical analysis revealed that Ago2 is present in a pre-miRNA processing complex that is able to transfer the miRNA into a target-mRNA cleaving complex, and these proteins are functionally required to mediate miRNA-guided mRNA cleavage. Expand
Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores
An essential cellular factor for nuclear mRNA export called Mex67p which has homologous proteins in human and Caenorhabditis elegans was identified through its genetic interaction with nucleoporin Nup85p, and is likely to participate directly in the export of mRNA from the nucleus to the cytoplasm. Expand
Crystal structure of the spliceosomal 15.5kD protein bound to a U4 snRNA fragment.
- I. Vidović, S. Nottrott, K. Hartmuth, R. Lührmann, R. Ficner
- Biology, Medicine
- Molecular cell
- 1 December 2000
The crystal structure of a spliceosomal RNP complex comprising the 15.5kD protein of the human U4/U6.U5 tri-snRNP and the 5' stem-loop of U4 snRNA is determined, giving an unusual RNA fold characterized by two tandem sheared G-A base pairs, a high degree of purine stacking, and the accommodation of a single RNA base in a pocket of the protein. Expand
A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies.
- M. Andrei, D. Ingelfinger, R. Heintzmann, T. Achsel, R. Rivera-Pomar, R. Lührmann
- Biology, Medicine
- 1 May 2005
RNAi-mediated knockdowns revealed that a subset of P body factors, including eIF4E-T, LSm1, rck/p54, and Ccr4 are required for the accumulation of each other and eif4E in P bodies, suggesting novel roles for these proteins in targeting mRNAs for 5' --> 3' degradation. Expand
The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci.
Coexpression of wild-type and mutant LSm proteins, as well as fluorescence resonance energy transfer studies, indicate that the mammalian proteins hLSm1-7 form a complex similar to the one found in yeast, and that complex formation is required for enrichment of the proteins in the cytoplasmic foci. Expand
A Common Core RNP Structure Shared between the Small Nucleoar Box C/D RNPs and the Spliceosomal U4 snRNP
The similarities in structure and function observed between the U4 snRNP (chaperone for U6) and the box C/D snoRNPs raises the interesting possibility that these particles may have evolved from a common ancestral RNP. Expand