Structure and mechanism of action of type IA DNA topoisomerases

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 st...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2009-12, Vol.74 (13), p.1467-1481
Main Authors: Bugreev, D. V, Nevinsky, G. A
Format: Article
Language:English
Subjects:
Animals
Archaeal Proteins - chemistry
Archaeal Proteins - genetics
Archaeal Proteins - metabolism
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding sites
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Cellular biology
Deoxyribonucleic acid
DNA
DNA Gyrase - chemistry
DNA Gyrase - metabolism
DNA Topoisomerases, Type I - chemistry
DNA Topoisomerases, Type I - classification
DNA Topoisomerases, Type I - genetics
DNA Topoisomerases, Type I - metabolism
DNA, Superhelical
Genomics
Humans
Life Sciences
Microbiology
Models, Molecular
Nucleic Acid Conformation
Protein Structure, Tertiary
Review
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Summary: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.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297909130045