Structure and mechanism of action of type IA DNA topoisomerases
- PMID: 20210704
- DOI: 10.1134/s0006297909130045
Structure and mechanism of action of type IA DNA topoisomerases
Abstract
DNA topoisomerases are enzymes responsible for regulation of genomic DNA supercoiling. They participate in essential processes of cells such as replication, transcription, recombination, repair, etc., and they are necessary for normal functioning of the cells. Topoisomerases alter the topological state of DNA by either passing one strand of the helix through the other strand (type I) or by passing a region of duplex DNA through another region of duplex DNA (type II). Type I DNA topoisomerases are subdivided into enzymes that bind to the 5'- (type IA) or 3'-phosphate group (type IB) during relaxation of the cleavable DNA. This review summarizes the literature on type IA DNA topoisomerases. Special attention is given to particular properties of their structure and mechanisms of functioning of these enzymes.
Similar articles
-
[DNA supercoiling and topoisomerases in Escherichia coli].Rev Latinoam Microbiol. 1995 Jul-Sep;37(3):291-304. Rev Latinoam Microbiol. 1995. PMID: 8850348 Review. Spanish.
-
Adenosine 5'-O-(3-thio)triphosphate (ATPgammaS) promotes positive supercoiling of DNA by T. maritima reverse gyrase.J Mol Biol. 2007 Aug 3;371(1):197-209. doi: 10.1016/j.jmb.2007.05.031. Epub 2007 May 18. J Mol Biol. 2007. PMID: 17560602
-
Structural insights into the function of type IB topoisomerases.Curr Opin Struct Biol. 1999 Feb;9(1):29-36. doi: 10.1016/s0959-440x(99)80005-0. Curr Opin Struct Biol. 1999. PMID: 10047584
-
The mechanism of negative DNA supercoiling: a cascade of DNA-induced conformational changes prepares gyrase for strand passage.DNA Repair (Amst). 2014 Apr;16:23-34. doi: 10.1016/j.dnarep.2014.01.011. Epub 2014 Feb 22. DNA Repair (Amst). 2014. PMID: 24674625 Review.
-
topIb, a phylogenetic hallmark gene of Thaumarchaeota encodes a functional eukaryote-like topoisomerase IB.Nucleic Acids Res. 2016 Apr 7;44(6):2795-805. doi: 10.1093/nar/gkw097. Epub 2016 Feb 22. Nucleic Acids Res. 2016. PMID: 26908651 Free PMC article.
Cited by
-
Review and Current Perspectives on DNA Topoisomerase I and II Enzymes of Fungi as Study Models for the Development of New Antifungal Drugs.J Fungi (Basel). 2024 Sep 3;10(9):629. doi: 10.3390/jof10090629. J Fungi (Basel). 2024. PMID: 39330389 Free PMC article. Review.
-
A highly processive actinobacterial topoisomerase I - thoughts on Streptomyces' demand for an enzyme with a unique C-terminal domain.Microbiology (Reading). 2020 Feb;166(2):120-128. doi: 10.1099/mic.0.000841. Epub 2019 Aug 7. Microbiology (Reading). 2020. PMID: 31390324 Free PMC article. Review.
-
Mechanistic insights from structure of Mycobacterium smegmatis topoisomerase I with ssDNA bound to both N- and C-terminal domains.Nucleic Acids Res. 2020 May 7;48(8):4448-4462. doi: 10.1093/nar/gkaa201. Nucleic Acids Res. 2020. PMID: 32232337 Free PMC article.
-
The many lives of type IA topoisomerases.J Biol Chem. 2020 May 15;295(20):7138-7153. doi: 10.1074/jbc.REV120.008286. Epub 2020 Apr 10. J Biol Chem. 2020. PMID: 32277049 Free PMC article. Review.
-
Topoisomerase I (TopA) is recruited to ParB complexes and is required for proper chromosome organization during Streptomyces coelicolor sporulation.J Bacteriol. 2013 Oct;195(19):4445-55. doi: 10.1128/JB.00798-13. Epub 2013 Aug 2. J Bacteriol. 2013. PMID: 23913317 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources