Carboxyl-terminal domain dimer interface mutant 434 repressors have altered dimerization and DNA binding specificities
- 13 November 1998
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 283 (5) , 931-946
- https://doi.org/10.1006/jmbi.1998.2136
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Dimerization of the UmuD' protein in solution and its implications for regulation of SOS mutagenesisNature Structural & Molecular Biology, 1997
- Recognition of Nonconserved Bases in the P22 Operator by P22 Repressor Requires Specific Interactions between Repressor and Conserved BasesPublished by Elsevier ,1997
- Dimerization specificity of P22 and 434 repressors is determined by multiple polypeptide segmentsJournal of Bacteriology, 1997
- Role of the C-Terminal Tail Region in the Self-Assembly of .lambda.-RepressorBiochemistry, 1995
- Expression, purification, and functional characterization of the carboxyl-terminal domain fragment of bacteriophage 434 repressorJournal of Bacteriology, 1994
- Operator Sequence Context Influences Amino Acid-Base-pair Interactions in 434 Repressor-Operator ComplexesJournal of Molecular Biology, 1993
- Amino acid similarities to other proteins offer insights into roles of UmuD and UmuC in mutagenesisGenome, 1989
- Recognition of a DNA Operator by the Repressor of Phage 434: A View at High ResolutionScience, 1988
- Torsional rigidity of DNA and length dependence of the free energy of DNA supercoilingJournal of Molecular Biology, 1984
- Stabilization of the hexameric form of Escherichia coli protein rho under ATP hydrolysis conditionsJournal of Molecular Biology, 1982