Single-molecule DREEM imaging reveals DNA wrapping around human mitochondrial single-stranded DNA binding protein
نویسندگان
چکیده
منابع مشابه
Single-molecule imaging reveals the mechanism of Exo1 regulation by single-stranded DNA binding proteins.
Exonuclease 1 (Exo1) is a 5'→3' exonuclease and 5'-flap endonuclease that plays a critical role in multiple eukaryotic DNA repair pathways. Exo1 processing at DNA nicks and double-strand breaks creates long stretches of single-stranded DNA, which are rapidly bound by replication protein A (RPA) and other single-stranded DNA binding proteins (SSBs). Here, we use single-molecule fluorescence imag...
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Single-stranded DNA-binding proteins (SSBs) play a key role in genome maintenance, binding and organizing single-stranded DNA (ssDNA) intermediates. Multimeric SSBs, such as the human mitochondrial SSB (HmtSSB), present multiple sites to interact with ssDNA, which has been shown in vitro to enable them to bind a variable number of single-stranded nucleotides depending on the salt and protein co...
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...
متن کاملStructural 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...
متن کاملBinding 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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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2018
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/gky875