Co-immunoprecipitation studies employing fragments of USP45 suggested that the non-catalytic 61 amino acids that lie prior to the Znf-UBP domain are necessary for binding to ERCC1, as truncation of these residues abolishes co-immunoprecipitation with endogenous ERCC1 (Fig 3A).
These minor groove contacts are essential for high-affinity DNA recognition by Kaiso as truncation of the CTE beyond ZF3 dramatically reduces the binding interaction.
As truncation of only the C-terminal residues did not prevent incorporation, the authors predicted that the N-terminal residues might play a role in rRNA binding.
Importantly, the C85 C105 mismatch, which has been proposed as a key determinant of small molecule ligand binding to the TS site 1 RNA [ 31, 32], is not an absolute requirement for hTS binding as none of the truncation mutants contained this motif.
To investigate the role of different putative NFκB binding sites, truncations of the SIRT1 promoter were generated.
The contribution of H1 domains to chromatin binding remains unclear, as truncation mutants can substitute for full-length H1 in some assays but also show reduced binding in living cells [7], [10], [11], [14], [15], [16], [17], [18].
HapX binds the 3′-submotif with low affinity (KD = 170.6 nM) as its binding was abolished by truncation of the 3′-submotif (compare second column in Fig 6B).
Therefore, NOD2-S seems to represent the shortest version of NOD2 with NLRP1 binding capacity, since further C-terminal truncations, apparently abrogate the binding, as exemplified by the absence of a detectable NLRP1 interaction for NOD2 1 163 and NOD2 1–135.
As discussed above, the truncation of the channel matrix omitted some channel coefficients.
VEGF109 arose accidentally as a PCR-generated truncation of VEGF165, and was retained for study.
