Movement and specificity in a modular DNA binding protein

Cary Liptak; J Patrick Loria

doi:10.1016/j.str.2015.05.004

Movement and specificity in a modular DNA binding protein

Structure. 2015 Jun 2;23(6):973-4. doi: 10.1016/j.str.2015.05.004.

Authors

Cary Liptak¹, J Patrick Loria²

Affiliations

¹ Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
² Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA; Department of Chemistry, Yale University, New Haven, CT 06520, USA. Electronic address: patrick.loria@yale.edu.

Abstract

The single-stranded DNA (ssDNA) binding protein RPA binds to and protects ssDNA while simultaneously recruiting numerous replication and repair proteins essential for genome integrity. In this issue of Structure, Brosey et al. (2015) show that the flexibility and interactions of the modular domains of RPA are altered by ssDNA binding and suggest that these changes in configurational freedom are important for the many functions of RPA.

Publication types

Comment

MeSH terms

DNA / metabolism*
Models, Molecular*
Replication Protein A / chemistry*
Replication Protein A / metabolism*

Substances

Replication Protein A
DNA

Abstract

Publication types

MeSH terms

Substances

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