This finding points to an assembly mechanism in which lectin domains may remain bound to receptors on the cell surface throughout assembly of the cytolytic toxin core and explains the hemagglutinating activity of purified toxin.
It may remain bound to the promoter, be released from the promoter, or be retained in the transcribing elongation complex.
While the σ may remain bound to the core enzyme and participate in transcription elongation, σ may only function in transcription initiation, and its release could trigger the transition of RNAP into the elongation phase.
Furthermore, our model explains the rapid movement of the Rvs167-GFP centroid upon scission: due to their affinity for curved membranes, the Rvs molecules are likely to first disassemble at the tubular part of the invagination that collapses after scission, while some of the Rvs molecules may remain bound to the membrane that forms the vesicle.
Yamamoto et al. (2007) based on the knowledge of two-step mechanism of the homoisocitrate dehydrogenase-catalyzed reaction claimed that a properly designed dead-end inhibitor, which cannot be decarboxylated, may remain bound at the enzyme active site and thus block it.
Next, we show that solutions remain bounded.
The states of the dynamic compensator remain bounded.
Once in active form, APC may or may not remain bound to EPCR, to which it has approximately the same affinity as the protein zymogen.
It is conceivable that if oligomerisation takes place between one normal peptide and one truncated peptide, transautophosphorylation may be not be possible and the normal CHEK2 molecules may still remain bound to the truncated molecules reducing the concentration of the active monomers to respond to DNA damage.
Together, these data would suggest that in the complex milieu of the retina, TRs may not remain bound to the rGH-PAL element, and that in the absence of high T3 a different factor(s) binds the sequence and recruits the appropriate co-activator components to drive reporter activity.
