Activation of the integrated stress response by stalled translation elongation complexes attenuates neurodegeneration, and demonstrates a protective link between a decrease in the rate of translation initiation and defects in translation elongation.
Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.
Quantification of all the major on- and off-pathway kinetic parameters in the transcription elongation cycle reveals that RNA polymerase II translocates slowly in a linear, non-branched Brownian ratchet mechanism.
Specific amino acids in the N-terminus of the replication initiator protein DnaA inhibit translation elongation upon carbon starvation, illustrating that the identity of the N-terminal amino acids of a protein can modulate protein synthesis yield under changing conditions.
NusG enhances transcription elongation by stabilizing DNA base pairs immediately upstream of the RNA-DNA hybrid but does not measurably affect the nucleotide incorporation and the forward translocation by RNA polymerase.
During initiation factor-independent RNA structure-driven translation initiation, a flexible RNA element drives the movement of a viral IRES through the ribosome's tRNA binding sites and promotes tRNA binding.