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J Mol Biol ; 427(4): 756-762, 2015 Feb 27.
Article in English | MEDLINE | ID: mdl-25433126

ABSTRACT

The single-stranded DNA (ssDNA)/RNA binding protein translin was suggested to be involved in chromosomal translocations, telomere metabolism, and mRNA transport and translation. Oligonucleotide binding surfaces map within a closed cavity of translin octameric barrels, raising the question as to how DNA/RNA gain access to this inner cavity, particularly given that, to date, none of the barrel structures reported hint to an entryway. Here, we argue against a mechanism by which translin octamers may "dissociate and reassemble" upon RNA binding and report a novel "open"-barrel structure of human translin revealing a feasible DNA/RNA entryway into the cavity. Additionally, we report that translin not only is confined to binding of ssDNA oligonucleotides, or single-stranded extensions of double-stranded DNA (dsDNA), but also can bind single-stranded sequences internally embedded in dsDNA molecules.


Subject(s)
DNA, Single-Stranded/chemistry , DNA-Binding Proteins/chemistry , RNA-Binding Proteins/chemistry , Animals , Binding Sites , Chromatography, Gel , Crystallography, X-Ray , DNA, Single-Stranded/ultrastructure , DNA-Binding Proteins/ultrastructure , Humans , Mice , Protein Binding , Protein Structure, Secondary , Protein Structure, Tertiary , RNA-Binding Proteins/ultrastructure , X-Ray Diffraction
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