The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration.
Open accessAbstract
The binding properties of the Escherichia coli encoded single strand binding protein (SSB) to a variety of synthetic homopolynucleotides, as well as to single stranded M13 DNA, have been examined as a function of the NaCl concentration (25.0 degrees C, pH 8.1). Quenching of the intrinsic tryptophan fluorescence of the SSB protein by the nucleic acid is used to monitor binding. We find that the site size (n) for binding of SSB to all single stranded nucleic acids is quite dependent on the NaCl concentration. For SSB-poly(dT), n = 33 +/- 3 nucleotides/tetramer below 10 mM NaCl and 65 +/- 5 nucleotides/tetramer above 0.20 M NaCl (up to 5 M). Between 10 mM and 0.2 M NaCl, the apparent site size increases continuously with [NaCl]. The extent of quenching of the bound SSB fluorescence by poly(dT) also displays two-state behavior, 51 +/- 3% quenching below 10 mM NaCl and 83 +/- 3% quenching at high [NaCl] (greater than 01.-0.2 M NaCl), which correlates with the observed changes in the occluded site size. On the basis of these observations as well as the data of Krauss et al. (Krauss, G., Sindermann, H., Schomburg, U., and Maass, G. (1981) Biochemistry 20, 5346-5352) and Chrysogelos and Griffith (Chrysogelos, S., and Griffith, J. (1982) Proc. Natl. Acad. Sci. U. S. A. 79,5803-5807) we propose a model in which E. coli SSB binds to single stranded nucleic acids in two binding modes, a low salt mode (n = 33 +/- 3), referred to as (SSB)33, in which the nucleic acid interacts with only two protomers of the tetramer, and one at higher [NaCl], n = 65 +/- 5, (SSB)65, in which the nucleic acid interacts with all 4 protomers of the tetramer. At intermediate NaCl concentrations a mixture of these two binding modes exists which explains the variable site sizes and other apparent discrepancies previously reported for SSB binding. The transition between the two binding modes is reversible, although the kinetics are slow, and it is modulated by NaCl concentrations within the physiological range. We suggest that SSB may utilize both binding modes in its range of functions (replication, recombination, repair) and that in vivo changes in the ionic media may play a role in regulating some of these processes.
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Cites
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Self-citationPlasmid vectors for high-efficiency expression controlled by the promoter of coliphage lambda
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Cited by
Biochemistry of homologous recombination in Escherichia coli
Kowalczykowski, S. C., Dixon, D. A., Eggleston, A. K., Lauder, S. D., & Rehrauer, W. M. (1994) · Microbiological Reviews · doi:10.1128/mr.58.3.401-465.1994 · Cited by 1,250
SSB as an Organizer/Mobilizer of Genome Maintenance Complexes
Shereda, R. D., Kozlov, A. G., Lohman, T. M., Cox, M. M., & Keck, J. L. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230802341296 · Cited by 553
Self-citationSelective inhibition of mutant human mitochondrial DNA replication in vitro by peptide nucleic acids
Taylor, R. W., Chinnery, P. F., Turnbull, D. M., & Lightowlers, R. N. (1997) · Nature Genetics · doi:10.1038/ng0297-212 · Cited by 249
Chen, A. F., Parks, B., Kathiria, A. S., Ober-Reynolds, B., Goronzy, J. J., & Greenleaf, W. J. (2022) · Nature Methods · doi:10.1038/s41592-022-01461-y · Cited by 139
Metadata
- Authors
- Lohman, T. M., & Overman, L. B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1985-03
- Volume
- 260
- Issue
- 6
- Pages
- 3594-3603
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1559132509
- Cited by
- 364
- References
- 27
- FWCI
- 4.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
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