This would be consistent with a role for the conserved SAP domain in mediating contact with the damaged substrate DNA, as has been proposed for other proteins possessing this domain [32].
However, because P110 lies in the 'latching loop' region of eukaryotic Mre11 that is likely to mediate contacts with Xrs2 (Schiller et al, 2012), sae2Δ suppression by this mutation might arise through altering such contacts.
In the case of these direct (AMPA-R mediated) contacts with motor neurons, prediction errors could only be generated by post-synaptic inhibition of those motor neurons by sensory afferent interneurons: see for example the left panel of Fig. 2.
In this regard, we note that the site of one of the sae2∆ suppressors, P110, lies in the 'latching loop' region of eukaryotic Mre11 that is likely to mediate contacts with Xrs2 (Schiller et al, 2012), suggesting that, in this case, sae2Δ suppression might arise through weakening this interaction and dampening Tel1 activity.
These results reinforce the importance of the perturbation ΔF508 causes in the surface topography of NBD1 in a region likely to mediate contact with the transmembrane domains of CFTR.
In most of the recruitment settings, young adults were asked to participate in the study by a staff member who mediated contact with the researcher.
While these various specializations likely mediate contacts with other cells or substrates, their functions and mechanisms are of course at this point unclear.
The active site of the deoxyribonuclease (DNase) activity is also required for ribonuclease (RNase) activity of BGLF5 in vitro [8], although the identification of single function mutants that retain DNase activity and lack shutoff and vice versa [3], [9] indicates that additional residues mediate contacts with viral or cellular factors, or the nucleic acids themselves, to specify the substrate.
DOI: http://dx.doi.org/10.7554/eLife.00327.009 Many hydrophobic and aromatic residues in CycT1 mediate contacts with AFF4.
A final potential scenario for the XLF XRCC4 Ligase IV complex, which does not envision interactions between XLF and XRCC4 homodimers, involves the possibility that XLF forms a heterodimer with XRCC4, and that such a heterodimer mediates contacts with Ligase IV together).
