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- W2794497310 endingPage "111" @default.
- W2794497310 startingPage "102" @default.
- W2794497310 abstract "Single stranded DNA binding proteins (SSB) are essential to the cell as they stabilize transiently open single stranded DNA (ssDNA) intermediates, recruit appropriate DNA metabolism proteins, and coordinate fundamental processes such as replication, repair and recombination. Escherichia coli single stranded DNA binding protein (EcSSB) has long served as the prototype for the study of SSB function. The structure, functions, and DNA binding properties of EcSSB are well established: The protein is a stable homotetramer with each subunit possessing an N-terminal DNA binding core, a C-terminal protein-protein interaction tail, and an intervening intrinsically disordered linker (IDL). EcSSB wraps ssDNA in multiple DNA binding modes and can diffuse along DNA to remove secondary structures and remodel other protein-DNA complexes. This review provides an update on these features based on recent findings, with special emphasis on the functional and mechanistic relevance of the IDL and DNA binding modes." @default.
- W2794497310 created "2018-04-06" @default.
- W2794497310 creator A5017864586 @default.
- W2794497310 creator A5083534168 @default.
- W2794497310 date "2019-02-01" @default.
- W2794497310 modified "2023-10-17" @default.
- W2794497310 title "Dynamics of E. coli single stranded DNA binding (SSB) protein-DNA complexes" @default.
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