TY - JOUR
T1 - Single-Stranded DNA Binding Proteins
AU - Kowalczykowski, Stephen C.
AU - Bear, David G.
AU - Von Hippel, Peter H.
N1 - Funding Information:
We are pleased to acknowledge many conversations with colleagues, both at the University of Oregon and elsewhere, that have helped to focus our thinking and improve our understanding of the subject matter of this review. We are also grateful to many colleagues, including Drs. Bruce Alberts, Rae Lynn Burke, Joseph Coleman, Malcolm Gefter, Larry Gold, Jack Grfith, Junko Hosoda, Richard Karpel, William Konigsberg, Timothy Lohman, Alexander McPherson, Thomas Record, Kenneth Williams and Samuel Wilson, who provided unpublished data or preprints of their relevant papers prior to publication. We wish to thank Ms. Nancy Caretto, who patiently typed and retyped the many drafts of this review. The research described here that has been carried out in our laboratory has been supported, in part, by U.S. Public Health Services Research Grant GM-15792, American Cancer Society Postdoctoral Fellowship PF-1301 (to S. Kowalczykowski) and USPHS Postdoctoral Fellowship GM-06676 (to D. Bear).
PY - 1981/1/1
Y1 - 1981/1/1
N2 - This chapter focuses on the proteins that bind preferentially and nonspecifically to single-stranded DNA and have no other (enzymatic) activity. These proteins are essential to many physiological functions, including replication, recombination, and repair, in a host of organisms ranging from bacteriophage to higher eukaryotes. Thus, single-stranded DNA binding proteins represent systems that have evolved substantially beyond primitive precursors, which may only have been capable of direct and uncontrolled nucleic acid binding. The chapter describes molecular aspects of the involvement of DNA binding proteins in entire systems of DNA replication, recombination, and repair. Nature and measurement of DNA–protein interactions along with general purification strategies for single-stranded DNA binding proteins are also presented. In addition, the chapter discusses the ways in which the single-stranded DNA binding proteins have been exploited as tools in molecular biological research, particularly in the electron microscopy of biological macromolecules and in certain biochemical assays. All DNA binding proteins seem to operate stoichiometrically (as opposed to catalytically), in that they are present at intracellular levels sufficient to effectively saturate the single-stranded DNA intermediates produced during replication, recombination, and repair. Binding cooperativity is essential in permitting complete coverage of single-stranded sequences and also in effectively destabilizing the small duplex hairpins formed by intrastrand base pairing in single-stranded DNA.
AB - This chapter focuses on the proteins that bind preferentially and nonspecifically to single-stranded DNA and have no other (enzymatic) activity. These proteins are essential to many physiological functions, including replication, recombination, and repair, in a host of organisms ranging from bacteriophage to higher eukaryotes. Thus, single-stranded DNA binding proteins represent systems that have evolved substantially beyond primitive precursors, which may only have been capable of direct and uncontrolled nucleic acid binding. The chapter describes molecular aspects of the involvement of DNA binding proteins in entire systems of DNA replication, recombination, and repair. Nature and measurement of DNA–protein interactions along with general purification strategies for single-stranded DNA binding proteins are also presented. In addition, the chapter discusses the ways in which the single-stranded DNA binding proteins have been exploited as tools in molecular biological research, particularly in the electron microscopy of biological macromolecules and in certain biochemical assays. All DNA binding proteins seem to operate stoichiometrically (as opposed to catalytically), in that they are present at intracellular levels sufficient to effectively saturate the single-stranded DNA intermediates produced during replication, recombination, and repair. Binding cooperativity is essential in permitting complete coverage of single-stranded sequences and also in effectively destabilizing the small duplex hairpins formed by intrastrand base pairing in single-stranded DNA.
UR - http://www.scopus.com/inward/record.url?scp=77956910754&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77956910754&partnerID=8YFLogxK
U2 - 10.1016/S1874-6047(08)60347-9
DO - 10.1016/S1874-6047(08)60347-9
M3 - Article
AN - SCOPUS:77956910754
SN - 1874-6047
VL - 14
SP - 373
EP - 444
JO - Enzymes
JF - Enzymes
IS - C
ER -