Molecular basis of DNA sequence recognition by the catabolite gene activator protein: detailed inferences from three mutations that alter DNA sequence specificity.
Open Access
- 1 December 1984
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 81 (23), 7274-7278
- https://doi.org/10.1073/pnas.81.23.7274
Abstract
Substitution of Glu-181 of the catabolite gene activator protein (CAP) by lysine, leucine or valine results in a protein that has specificity for A.cntdot.TR base pairs at positions 7 and 16 of the DNA recognition site, rather than G.cntdot.C base pairs as is the case with the wild-type CAP. From these genetic data are deduced both the specifc chemical interactions by which amino acid side chains at position 181 interact with base pairs 7 and 16 and the precise alignment between the structures of the CAP and DNA in the intermolecular CAP-DNA complex. The 2 symmetry-related F .alpha.-helices of the CAP dimer probably interact with successive major grooves of right-handed B-type DNA.This publication has 39 references indexed in Scilit:
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