Transient binding of all these components might protect the head-platform interface in a chaperone-like way from non-productive interactions with abundant cytosolic (translation related) factors, thereby opening a time window for final folding, and eventually assembly events, which could be further actively promoted by Prp43p's RNA helicase activity.
Therefore, conventional methods are difficult to determine the binding degrees of these components with plasma proteins.
In general, acetylation of the N-terminal histone tails is a dominant signal for active chromatin facilitating the binding of the components of the basal transcription machinery.
Ribosomal rRNA U1963 is a crucial residue within the overlapping binding sites of RRF, EF-G, and the P-site tRNA suggesting a plausible mechanism of translation inhibition by inhibiting the binding of these critical translation components.
Importantly, knockdown and overexpression of these nucleoporins, respectively, decrease and increase the expression of the target genes, strengthening the view that binding of these dynamic NPC components to the genes directly affects transcription (Capelson et al. 2010; Kalverda et al. 2010; Vaquerizas et al. 2010; Light et al. 2013; Ptak et al. 2014).
We observe that treatment of the ePTFE surface with acidified buffer facilitates binding of OptiMat components to these synthetic grafts.
Despite evidence for α-helical binding motifs for some of these components (Pex13p, Pex14p) its overall appearance is that of a molten globule and folding/unfolding transitions may play a critical role in its function.
These proteins affect binding of spliceosomal components to the splice sites and thus spliceosome formation [6].
These experiments suggest that Ki-67 directs the binding of nucleolar components to the chromosome periphery, perhaps by acting as a scaffold.
