An ancient complex comprising the eukaryotic elongation factor-1A and aminoacylated tRNA is shown to be the target of a cyclic heptapeptide and two unrelated natural products with potent anticancer activity.
Drosophila has almost all transcription factor binding specificities available to humans; and human transcription factors with divergent specificities operate in cell types that are not found in fruit flies.
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.
The hypoxia-inducible factor HIF drives transcription of the gene cyp-36A1, which encodes a cytochrome P450 enzyme that acts via a putative intercellular signal to regulate the nuclear receptor NHR-46 and consequently stress resistance and behavior.
Fibroblast growth factor induces dephosphorylation and inactivation of the NPR2 guanylyl cyclase, thus decreasing cyclic GMP production in growth plate chondrocytes and contributing to FGF-dependent decreases in bone growth.
Experimental mapping of the joint sequence space of an ancient transcription factor (TF) and its DNA binding sites reveals that epistasis across the molecular interface permitted the evolution of a new and specific TF-DNA complex.