Structural dynamics of E . coli single - stranded DNA binding protein 1 reveal DNA wrapping and unwrapping pathways
نویسندگان
چکیده
Affiliations: 5 Department of Physics, Center for the Physics of Living Cells, and Center for Biophysics and 6 Computational Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA. 7 Department of Biochemistry and Molecular Biophysics, Washington University School of 8 Medicine, St. Louis, Missouri, USA. 9 *Correspondence to: [email protected] and [email protected] 10 11
منابع مشابه
Structural dynamics of E. coli single-stranded DNA binding protein reveal DNA wrapping and unwrapping pathways
Escherichia coli single-stranded (ss)DNA binding (SSB) protein mediates genome maintenance processes by regulating access to ssDNA. This homotetrameric protein wraps ssDNA in multiple distinct binding modes that may be used selectively in different DNA processes, and whose detailed wrapping topologies remain speculative. Here, we used single-molecule force and fluorescence spectroscopy to inves...
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The Escherichia coli single-stranded DNA binding protein (SSB) binds selectively to single-stranded (ss) DNA intermediates during DNA replication, recombination and repair. Each subunit of the homo-tetrameric protein contains a potential ssDNA binding site, thus the protein can bind to ssDNA in multiple binding modes, one of which is the (SSB)(65) mode, in which a 65 nucleotide stretch of ssDNA...
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Wrapping of genomic DNA into nucleosomes poses thermodynamic and kinetic barriers to biological processes such as replication, transcription, repair and recombination. Previous biochemical studies have demonstrated that in the presence of adenosine triphosphate (ATP) the human RAD51 (HsRAD51) recombinase can form a nucleoprotein filament (NPF) on double-stranded DNA (dsDNA) that is capable of u...
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Escherichia coli single-stranded DNA (ssDNA) binding protein (SSB) is the defining bacterial member of ssDNA binding proteins essential for DNA maintenance. SSB binds ssDNA with a variable footprint of ∼30-70 nucleotides, reflecting partial or full wrapping of ssDNA around a tetramer of SSB. We directly imaged single molecules of SSB-coated ssDNA using total internal reflection fluorescence (TI...
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ABSTRACT In eukaryote cells, DNA is complexed with a series of basic proteins making units of chromatin structure named nucleosomes. In addition, nonhistone proteins with different function are the components of chromatin. Among these proteins, a group with a low mobility on gel electrophoresis have been identified and named LMG. In this study a LMG protein with a molecular weigh of 160 ...
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