Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.
Open accessAbstract
The DNA binding properties of 52 different single-amino acid substitutions in lambda repressor's amino-terminal domain have been characterized. Seven proteins bearing mutations that change solvent-exposed side chains have been purified. The amino-terminal domains of these mutant repressors are folded and are comparable to the wild-type amino-terminal domain in thermal stability. In contrast, a purified mutant repressor bearing a substitution in a buried side chain contains an amino-terminal domain with decreased thermal stability. We argue that mutations that alter solvent-exposed wild-type side chains define residues that form the operator DNA binding surface of lambda repressor whereas completely or partially buried mutations exert their effect by decreasing protein stability.
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QL44 and IS84 are mutations in the DNA-binding domain of λ repressor that act as dominant negative alleles in intact λ repressor.
“QL44 and IS84 are mutations in the DNA-binding domain of λ repressor that act as dominant negative alleles in intact λ repressor (Hecht et al., 1983; Nelson et al., 1983).”
From Oligomerization properties of GCN4 leucine zipper <i>e</i> and <i>g</i> position mutants (1997) · cites this paper as Hecht et al., 1983
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Oligomerization properties of GCN4 leucine zipper <i>e</i> and <i>g</i> position mutants
Zeng, X., Zhu, H., Lashel, H. A., & Hu, J. C. (1997) · Protein Science · doi:10.1002/pro.5560061016 · Cited by 50 · see citing works
- Authors
- Hecht, M. H., Nelson, H. C., & Sauer, R. T.
- Affiliations
- Massachusetts Institute of Technology (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1983-05
- Volume
- 80
- Issue
- 9
- Pages
- 2676-2680
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC393890
- OpenAlex
- W1972412311
- Cited by
- 137
- References
- 0
- Citations by year
- 2020: 1 · 2019: 3 · 2018: 1 · 2017: 1 · 2014: 1 · 2013: 2 · 2012: 1
- FWCI
- 8.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- lambda repressor, N-terminal domain, single amino acid substitution, protein stability, thermal stability, DNA binding, protein folding, bacteriophage lambda
- MeSH terms
- Amino Acid Sequence, Base Sequence, DNA-Binding Proteins, DNA, Viral, Models, Molecular, Mutation, Bacteriophage lambda, Protein Conformation, Repressor Proteins, Structure-Activity Relationship, Thermolysin, Transcription Factors, Viral Proteins, Viral Regulatory and Accessory Proteins
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