Suggestions(1)
Exact(3)
Data that support this viewpoint are as follows: (1) Like DNA chaperones such as HU and HMGB1, tau protein binds to the minor groove of DNA, without nucleotide sequence specificity.
In addition, DNA isomerases, DNA chaperones and accessory proteins also regulate DNA access, coiling, bending and packing.
However, the precisely spatial and temporal assembly and disassembly of these structures require the G4 DNA chaperones and resolvases.
Similar(57)
HMGB1 is a DNA chaperone concentrated in the cell nucleus first demonstrated to induce cell migration and differentiation.
These observations suggest that the interaction of tau protein with DNA is similar to a DNA chaperone.
Tau protein seems to act in a DNA chaperone-like manner in the association with the DNA double-strand.
Another DNA chaperone HMGB1 also bends the double-strand and binds in a beads-on-a-string manner without sequence specificity [48].
High-mobility group box 1 (HMGB1) is a nuclear protein that binds to DNA functioning as a DNA chaperone.
HMGB1 is normally located in the nucleus, acting as a DNA chaperone involved in the regulation of a number of DNA-associated processes such as replication, transcription, recombination, and repair.
UP1 has been shown to bind and destabilize G-quadruplex structures and potentially serve as a DNA chaperone responsible for the unfolding of the G-quadruplex structure into single-stranded DNA to facilitate the binding of telomerase for lengthening of the telomere.
Indeed, GroEL1 of M. tuberculosis was recently identified as being associated with nucleotides, suggesting a role as a DNA chaperone, while GroEL1 of M. smegmatis was found to have a role in mycolic acid biosynthesis during biofilm formation [ 5, 6, 3].
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