Thermodynamic analysis of DNA binding by a Bacillus single stranded DNA binding protein
نویسندگان
چکیده
منابع مشابه
Binding of the dimeric Deinococcus radiodurans single-stranded DNA binding protein to single-stranded DNA.
Deinococcus radiodurans single-stranded (ss) DNA binding protein (DrSSB) originates from a radiation-resistant bacterium and participates in DNA recombination, replication, and repair. Although it functions as a homodimer, it contains four DNA binding domains (OB-folds) and thus is structurally similar to the Escherichia coli SSB (EcoSSB) homotetramer. We examined the equilibrium binding of DrS...
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The homotetrameric Escherichia coli single-stranded DNA-binding (SSB) protein plays a central role in DNA replication, repair, and recombination. In addition to its essential activity of binding to transiently formed single-stranded (ss) DNA, SSB also binds an array of partner proteins and recruits them to their sites of action using its four intrinsically disordered C-terminal tails. Here we s...
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The emergence of DNA as the predominant hereditary material of life has necessitated the evolution of proteins whose sole function is the maintenance and care of these vital molecules. In a typical cell, there is a wide array of proteins with specialized functions in DNA metabolism that allow the cell to maintain and replicate its genome. In order to copy or make repairs to DNA, the double heli...
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Single-stranded DNA (ssDNA) is a product of many cellular processes that involve double-stranded DNA, for example during DNA replication and repair, and is formed transiently in many others. Measurement of ssDNA formation is fundamental for understanding many such processes. The availability of a fluorescent biosensor for the determination of single-stranded DNA provides an important route to a...
متن کاملCharacterization of a mitochondrial protein binding to single-stranded DNA.
A DNA-binding protein from Xenopus laevis oocyte mitochondria which has been found associated with the D-loop also shows a strong preference for single-stranded DNA. The binding to polynucleotides is dependent on the base composition, but no sequence specificity was found. This protein, called mtSSB, binds tightly and cooperatively to single-stranded DNA. By its amino-acid composition and its b...
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ژورنال
عنوان ژورنال: BMC Biochemistry
سال: 2012
ISSN: 1471-2091
DOI: 10.1186/1471-2091-13-10