Archaebacterial reverse gyrase cleavage-site specificity is similar to that of eubacterial DNA topoisomerases I

ATP-dependent type I topoisomerases from extremely thermophilic archaebacteria--reverse gyrases--drive positive supercoiling of DNA. We showed that reverse gyrase from Desulfurococcus amylolyticus breaks the DNA at specific sites and covalently binds to the 5' end. In 30 out of 31 sites located...

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Bibliographic Details
Published in:Nucleic acids research 1990-05, Vol.18 (9), p.2801-2805
Main Authors: KOVALSKY, O. I, KOZYAVKIN, S. A, SLESAREV, A. I
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Archaea - enzymology
Bacteria - enzymology
Base Sequence
Biological and medical sciences
Densitometry
Desulfurococcus
DNA Topoisomerases, Type I - metabolism
DNA Topoisomerases, Type II - metabolism
DNA, Bacterial - metabolism
Electrophoresis, Polyacrylamide Gel
Enzymes and enzyme inhibitors
Escherichia coli - enzymology
Fundamental and applied biological sciences. Psychology
Isomerases
Micrococcus - enzymology
Molecular Sequence Data
Substrate Specificity
Temperature
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Summary:ATP-dependent type I topoisomerases from extremely thermophilic archaebacteria--reverse gyrases--drive positive supercoiling of DNA. We showed that reverse gyrase from Desulfurococcus amylolyticus breaks the DNA at specific sites and covalently binds to the 5' end. In 30 out of 31 sites located in pBR322 DNA fragments, cleavage occurs at the sequence 5'---CNNN/---(N is any base). The same rule was previously shown to hold for single-stranded DNA breakage by eubacterial topoisomerases I. The relative cleavage frequencies at different sites depend on Mg2+ and temperature. We discuss the possible physiological and mechanistic role of the above specificity of the bacterial topoisomerases I.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/18.9.2801