The interaction with DNA of wild-type and mutant fushi tarazu homeodomains.

摘要: The in vitro DNA binding properties of wild-type and mutant fushi tarazu homeodomains (ftz HD) have been analysed. the ftz HD are very similar to those Antp HD. In interference experiments with HDs, close approaches between specific portions peptide regions site were mapped. A methylation interference, G7 on beta strand BS2, is absent from pattern a [ftz (R43A) HD] which Arg43 at second position helix III (the recognition helix) replaced by an Ala. This indicated that proximity N7 BS2 major groove. ethylation patterns (NTD) HD, first six amino acids homeodomain deleted, extensively altered relative patterns. Methylation A11 G12 alpha phosphate nucleotide A12 no longer interfere binding. interact minor groove, A13 adjacent groove BS2. study using change specificity mutation (Q50K) HD], Gln50 ninth third exchanged for Lys (as bicoid HD), variant sites, we concluded 50 peptides interacts base pairs positions 6 7 These three points contact allowed us propose crude orientation within protein-DNA complex. We find way.