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A new study reveals that extracellular signals can activate a signal-transduction cascade that simultaneously alters alternative splicing and translation of the same target. These concerted efforts probably serve to increase the speed and strength of the cellular response to changes in the extracellular environment.
Eukaryotic messenger RNAs are degraded through a pathway that starts with the removal of the poly(A) tail. A recent study shows that cytoplasmic mRNA deadenylation in mammals occurs by the consecutive action of two distinct deadenylases and that degradation of nonsense mRNA involves the same biphasic deadenylation pathway.
A new study sheds light on the mechanism regulating the translation of localized mRNAs at their destination. Phosphorylation of an RNA-binding protein by Src promotes complex disassembly and allows translation of the localized transcript.
The induction and repair of chromosome breaks is associated with myriad changes in chromatin. A recent study shows that chromatin remodeling that results in histone eviction at the break site requires the Mre11 complex and INO80 and that these events are important for efficient loading of the Rad51 recombinase.
A recent structural study on a human RNA deaminase reveals that inositol hexakisphosphate is a cofactor of the enzyme and is essential for its editing activity.
Flock House virus protein B2 suppresses the RNA-mediated interference response by binding double-stranded RNA of almost any size or sequence. The crystal structure of this protein bound to RNA reveals a novel fold that suggests its mechanism of action.
RNase P is an ancient ribonucleoprotein (RNP) enzyme present in every living organism. Several recent reports collectively provide a structural and functional analysis of this 'simple' RNP and result in a better understanding of the apparent differences between the two types of RNase P in bacteria.
Telomeres are crucial for maintaining the integrity of the genome. Several alternative structures have been proposed for these caps, and understanding their biological significance is a matter of great interest. Probing of native telomeres now reveals that telomere end-binding proteins may control the formation of G-quadruplex DNA in vivo.
How are individual transmembrane helices in polytopic membrane proteins delivered from the Sec translocon into the lipid bilayer? A new study on the aquaporin-4 water channel shows that they move out of the translocon in succession but may linger nearby for an extended period of time.
A recent study broadens the substrate profile of the COMPASS histone methyltransferase complex to include a kinetochore component and links the lysine methylation activity of COMPASS to the process of chromosome segregation.
The stress-activated protein kinases PKR and GCN2 regulate protein synthesis by phosphorylating the α subunit of translation initiation factor 2. Three recent studies reveal the molecular basis for the exquisite substrate specificity of this family of kinases and address the role of interlobe flexibility in kinase activation.
A new study adds to our understanding of the interconnection between different nuclear processes by showing that a 'classical' metazoan precursor mRNA–processing factor functions to prevent transcription-associated genomic instability.
