Photo CIDNP study on the complex formation of λ‐ cro protein with OR3
- 25 February 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 181 (2) , 286-290
- https://doi.org/10.1016/0014-5793(85)80277-5
Abstract
A photo CIDNP spectrum of λ cro repressor protein showed that one of the three tyrosines and His 35 are quite accessible to the photosensitive dye. For the remaining two tyrosine residues one is slightly accessible, but the other is inaccessible. In comparison with the result of differential nitration at tyrosine side chains followed by the peptide analysis, it can be concluded that Tyr 26 is mostly exposed and Tyr 51 is slightly exposed on the surface of the cro dimer. On the addition of OR3 17mer, His 35 and Tyr 26 are no longer accessible to the dye, which indicates that they are involved in interaction. However, a similar phenomenon was observed by adding CAP binding site 22mer. The interaction mechanism will be discussed.Keywords
This publication has 14 references indexed in Scilit:
- Plasmid vectors designed for high-efficiency expression controlled by the portable recA promoteroperator of Escherichia coliGene, 1984
- Comparison of the structures of Cro and λ repressor proteins from bacteriophage λJournal of Molecular Biology, 1983
- Crystallographic data for complexes of the Cro repressor with DNAJournal of Molecular Biology, 1983
- Studies of the structure of bacteriophage λ cro protein in solutionFEBS Letters, 1982
- The molecular basis of DNA–protein recognition inferred from the structure of cro repressorNature, 1982
- Homology among DNA-binding proteins suggests use of a conserved super-secondary structureNature, 1982
- Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor.Proceedings of the National Academy of Sciences, 1982
- Photo-CIDNP Studies of ProteinsPublished by Springer Nature ,1982
- λ Repressor and cro—components of an efficient molecular switchNature, 1981
- Structure of the cro repressor from bacteriophage λ and its interaction with DNANature, 1981