Document Type

Article

Language

eng

Publication Date

3-30-2018

Publisher

Elsevier

Source Publication

Seminars in Cell & Developmental Biology

Source ISSN

1084-9521

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.

Comments

Accepted version. Seminars in Cell & Developmental Biology, Vol. 56 (February 2019): 102-111. DOI. © 2018 Elsevier B.V. Used with permission.

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