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HuR and mRNA stability
The influence of newly identified protein ligands to HuR on HuR function in both normal and stressed cells may explain how ARE-mediated mRNA decay is regulated in response to environmental change.
Switching from Repression to Activation: MicroRNAs Can Up-Regulate Translation
It is proposed that translation regulation by microRNPs oscillates between repression and activation during the cell cycle, and two well-studied microRNAs—Let-7 and the synthetic microRNA miRcxcr4—likewise induce translation up-regulation of target mRNAs on cell cycle arrest.
Human Upf Proteins Target an mRNA for Nonsense-Mediated Decay When Bound Downstream of a Termination Codon
It is suggested that assembly of a dynamic hUpf complex initiates in the nucleus at mRNA exon-exon junctions and triggers NMD in the cytoplasm when recognized downstream of a translation termination site.
Monoclonal antibodies to nucleic acid-containing cellular constituents: probes for molecular biology and autoimmune disease.
The monoclonal anti-Sm antibody gives the same immunoprecipitation pattern, providing direct evidence that the Sm antigen resides on all these RNA-protein complexes, which will be valuable in deciphering the biological function of these ubiquitous small nuclear RNPs.
Overexpression of HuR, a nuclear–cytoplasmic shuttling protein, increases the in vivo stability of ARE‐containing mRNAs
HuR may initially bind to ARE‐containing mRNAs in the nucleus and provide protection during and after their export to the cytoplasmic compartment, establishing an in vivo role for HuR in mRNA decay.
SR splicing factors serve as adapter proteins for TAP-dependent mRNA export.
It is demonstrated that at least three shuttling SR (serine/arginine-rich) proteins interact with the same domain of TAP/NXF1 that binds REFs, which suggests multiple adapters including SR proteins most likely cooperate to recruit multiple copies of T AP/NxF1 for efficient mRNA export.
Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR
The results suggest that association with any position on a target mRNA is mechanistically sufficient for a microribonucleoprotein to exert repression of translation at some step downstream of initiation.
Identification of a sex-factor-affinity site in E. coli as gamma delta.
A conserved WD40 protein binds the Cajal body localization signal of scaRNP particles.
It is demonstrated that a requirement for WDR79 binding in the CB localization of a scaRNA is demonstrated, establishing WDR 79 as a central player in the localization and processing of nuclear RNPs.
Two small RNAs encoded by Epstein-Barr virus and complexed with protein are precipitated by antibodies from patients with systemic lupus erythematosus.
Primate cells harboring the Epstein-Barr virus (EBV) genome synthesize large amounts of two small RNAs:EBER 1 and EBER 2 (EBV-encoded RNA). These RNAs are approximately 180 nucleotides long, possess