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The Pumilio protein binds RNA through a conserved domain that defines a new class of RNA-binding proteins.
TheRNA-binding domain of PUM is shown to be an evolutionarily conserved, 334-amino acid region at the carboxy-terminus of the approximately 158-kDa PUM protein, which retains the RNA-binding specificity of full-length PUMprotein.
Dual modes of RNA-silencing suppression by Flock House virus protein B2
Results suggest that B2 blocks both cleavage of the FHV genome by Dicer and incorporation of FHv small interfering RNAs into the RNA-induced silencing complex.
α Helix-RNA Major Groove Recognition in an HIV-1 Rev Peptide-RRE RNA Complex
The solution structure of a human immunodeficiency virus type-1 (HIV-1) Rev peptide bound to stem-loop IIB of the Rev response element (RRE) RNA was solved by nuclear magnetic resonance spectroscopy.
An assembly landscape for the 30S ribosomal subunit
It is found that local transformations throughout the assembling subunit have similar but distinct activation energies, and the prevailing view of 30S assembly as a pathway proceeding through a global rate-limiting conformational change must give way to one in which the assembly of the complex traverses a landscape dotted with various local conformational transitions.
Assembly of bacterial ribosomes.
The history of the early work on ribosome assembly in Escherichia coli is presented, including a description of in vivo and in vitro intermediates, and the effects of ribosomal proteins in driving these events are explored.
Conformation of the TAR RNA-arginine complex by NMR spectroscopy.
The messenger RNAs of human immunodeficiency virus-1 (HIV-1) have an RNA hairpin structure, TAR, at their 5' ends that contains a six-n nucleotide loop and a three-nucleotide bulge that stabilizes arginine hydrogen bonding to G26 and phosphates.
Reduction of translating ribosomes enables Escherichia coli to maintain elongation rates during slow growth
It is established that the translational elongation rate decreases as growth slows, exhibiting a Michaelis–Menten dependence on the abundance of the cellular translational apparatus, however, an appreciable elongations rate is maintained even towards zero growth, including the stationary phase.
Inhibition of telomerase by G-quartet DMA structures
Folding of telomeric DNA into G-quartet structures seems to influence the extent of telomere elongation in vitro and might therefore act as a negative regulator of lengthening in vivo.
Quantitative analysis of protein-RNA interactions by gel mobility shift.
The quantitative application of the gel mobility shift assay to elucidate thermodynamic properties of protein-RNA complexes is reviewed and designs for titration, competition, and stoichiometry experiments are presented for two unrelated model complexes.
A CCHC metal‐binding domain in Nanos is essential for translational regulation
The Drosophila Nanos protein is a localized repressor of hunchback mRNA translation in the early embryo, and is required for the establishment of the anterior–posterior body axis, where it binds to RNA in vitro with high affinity, but with little sequence specificity.