A Dimeric Mutant of the Homotetrameric Single-Stranded DNA Binding Protein from Escherichia coli
Author:
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/BC.2002.151/pdf
Reference37 articles.
1. Modulation of the affinity of the single-stranded DNA-binding protein of Escherichia coli (E. coli SSB) to poly(dT) by site-directed mutagenesis
2. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
3. Tryptophan analysis of proteins in 6M guanidine hydrochloride: Modification for more general application
4. A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli single-strand binding protein-nucleic acid interactions
5. Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions
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1. A stable tetramer is not the only oligomeric state that mitochondrial single-stranded DNA binding proteins can adopt;Journal of Biological Chemistry;2019-03
2. The mitochondrial single-stranded DNA binding protein from S. cerevisiae, Rim1, does not form stable homo-tetramers and binds DNA as a dimer of dimers;Nucleic Acids Research;2018-06-21
3. Site-directed mutagenesis of the χ subunit of DNA polymerase III and single-stranded DNA-binding protein of E. coli reveals key residues for their interaction;Nucleic Acids Research;2010-10-22
4. Biophysical Analysis of Thermus aquaticus Single-Stranded DNA Binding Protein;Biophysical Journal;2008-03
5. 3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins;Nucleic Acids Research;2006-11-27
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