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• W2146258147 abstract "Hyperthermophilic organisms must protect their constituent macromolecules from heat-induced degradation. A general mechanism for thermoprotection of DNA in active cells is unknown. We show that reverse gyrase, the only protein that is both specific and common to all hyperthermophiles, reduces the rate of double-stranded DNA breakage approximately 8-fold at 90 degrees C. This activity does not require ATP hydrolysis and is independent of the positive supercoiling activity of the enzyme. Reverse gyrase has a minor nonspecific effect on the rate of depurination, and a major specific effect on the rate of double-strand breakage. Using electron microscopy, we show that reverse gyrase recognizes nicked DNA and recruits a protein coat to the site of damage through cooperative binding. Analogously to molecular chaperones that assist unfolded proteins, we found that reverse gyrase prevents inappropriate aggregation of denatured DNA regions and promotes correct annealing. We propose a model for a targeted protection mechanism in vivo in which reverse gyrase detects damaged DNA and acts as a molecular splint to prevent DNA breakage in the vicinity of the lesion, thus maintaining damaged DNA in a conformation that is amenable to repair." @default.
• W2146258147 created "2016-06-24" @default.
• W2146258147 creator A5043005286 @default.
• W2146258147 creator A5077510821 @default.
• W2146258147 date "2004-07-07" @default.
• W2146258147 modified "2023-09-26" @default.
• W2146258147 title "Reverse gyrase has heat-protective DNA chaperone activity independent of supercoiling" @default.
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• W2146258147 doi "https://doi.org/10.1093/nar/gkh683" @default.
• W2146258147 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/484171" @default.
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• W2146258147 hasPublicationYear "2004" @default.
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