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- W2092121035 abstract "A series of C- and N-terminal deletion mutants of Escherichia coli single-stranded DNA binding protein (SSB) was constructed, purified, and characterized in terms of ability to self-multimerize and to bind to DNA. High-performance gel filtration chromatography revealed that the amino acids 89−105 play a key role in the maintenance of homotetramer for native SSB of 177 amino acids. Interestingly, all of the N-terminal deletion mutants studied here were eluted as octamers, indicating that the N-terminal 11 residues are involved in the prevention of the formation of octamers. The binding of SSB and its deletion mutant proteins to single-stranded d(T)n was examined by gel mobility shift assay and circular dichroism spectroscopy. C-terminal deletion mutant proteins, SSB1−135 and SSB1−115, maintained high affinity and may be wrapped by single-stranded DNA (ssDNA) in the same way as in the case of native SSB. In contrast, deletion of the C-terminal region (residues 89−115) or N-terminal region (residues 1−11) caused a dramatic decrease in the binding affinity. Furthermore, two different stoichiometries of SSB in the complexes with d(T)64, but not with d(T)32, were observed for native SSB, SSB1−135, SSB1−115, and SSB37−177, suggesting that the (SSB)65 and (SSB)35 binding modes, as previously demonstrated [Lohman, T. M., & Overman, L. B. (1985) J. Biol. Chem. 260, 3594−3603; Bujalowski, W., & Lohman, T. M. (1986) Biochemistry 25, 7799−7802], occurred at lower and higher SSB concentrations, respectively. A functional map for SSB molecule was presented and discussed." @default.
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- W2092121035 date "1997-06-01" @default.
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- W2092121035 title "Functional Domains of <i>Escherichia coli</i> Single-Stranded DNA Binding Protein As Assessed by Analyses of the Deletion Mutants" @default.
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- W2092121035 doi "https://doi.org/10.1021/bi961647s" @default.
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