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The F1 association would bring the whole talin head closer to the membrane, facilitating interactions between the basic patch on F2 and F3 and acidic membrane phospholipids.
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Intriguingly, the interaction between Dot1 and the basic patch on the histone H4 tail (which is also bound by Sir3 [ 26, 27]) is not sufficient to trigger methyltransferase-independent derepression, as LexA-Dot1172-580 G401R, which lacks the N terminus but still contains the C-terminal H4-binding domain, failed to derepress.
Due to the topological difference between ATRXDBM and RASSF1CDBM, the basic C-terminal tail of RASSF1CDBM is close to the basic patch of DAXXDHB, which is where the acidic N-terminal extension of ATRXDBM binds (Fig. 2E and 2G).
The proposed model of CARD-CARD and PYD-PYD interactions is that the acidic patch of one domain interacts with the basic patch of the other protein.
(A ) The basic patch of RanQLGTP contributes to Slx9 binding.
This interaction depends on the basic patch of RanGTP.
Altogether, these results suggest that, similar to Kap123, Slx9 binding to RanQLGTP involves the basic patch.
The basic patch and acidic tail of Ran modulates interactions with Slx9.
The difference in DNA-binding affinity between ΔBP1 and SYCP3Core, which includes BP2 but not BP1, suggests that additional amino acids surrounding the basic patch residues contribute to DNA binding.
The C-terminal domain (Dot1) harbors the catalytic activity and the acidic patch that binds to the basic patch on the tail of histone H4 [ 26, 27, 52].
In the case of mutant K285E, the replacement of a basic amino acid by an acidic one masks the basic patch located in this area.
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