Recruitment of the Cyc8 Tup1 complex, which has no DNA binding activity, is directed by promoter-specific DNA binding factors such as α2-Mcm1p, Crt1p, Mig1p, Rox1p, and Sfl1p [7–9].
The binding of guide RNA is directed by its conserved secondary structure and sequence motifs, which enables guide RNA with different sequences to be incorporated into the same protein complex.
Since DC migration is directed by CCL21 binding to CCR7 on DCs and we observed direct binding of CCL21 to sialic acids, we hypothesized that polySia on mDCs might promote DC migration towards CCL21.
This structure suggests that DNA binding by pol λ is directed predominantly by the 8 kDa domain, which anchors the polymerase at the 5′-end regardless of the conformation of the 3′-end.
We used ChIP followed by sequencing (Table S1 available online) to determine CTCF binding in livers isolated from five eutherian mammals (human, macaque, mouse, rat, and dog) and the metatherian gray short-tailed opossum and confirmed that CTCF binding is mainly directed by genetic sequence rather than nuclear environment (Wilson et al., 2008).
In mammalian cells, the Ccr4-Not complex is also recruited to microRNA (miRNA) targets through interactions with the GW182 protein, which in turn is directed to miRNA binding sites by argonaute proteins [ 12– 12].
This regulation could either be direct (by direct binding of divalent cations to Zur, thereby changing the conformation of the regulator) or indirect (by lowering the intracellular Zn levels), as suggested previously [ 45, 47].
It was previously reported that GABARAP binds to microfilaments (actin) as well as microtubules (β-tubulin); the actin binding is not direct, and it may be mediated by yet unknown proteins (Wang and Olsen, 2000).
The dsDNA binding activity of TRF2 is primarily directed by its C-terminal Myb domain.
