InterPro : IPR013758

Name  DNA topoisomerase, type IIA, subunit A/ C-terminal, alpha-beta Short Name  Topo_IIA_A/C_ab
Type  Domain Description  DNA topoisomerases regulate the number of topological links between two DNA strands (i.e. change the number of superhelical turns) by catalysing transient single- or double-strand breaks, crossing the strands through one another, then resealing the breaks []. These enzymes have several functions: to remove DNA supercoils during transcription and DNA replication; for strand breakage during recombination; for chromosome condensation; and to disentangle intertwined DNA during mitosis [, ]. DNA topoisomerases are divided into two classes: type I enzymes (; topoisomerases I, III and V) break single-strand DNA, and type II enzymes (; topoisomerases II, IV and VI) break double-strand DNA [].Type II topoisomerases are ATP-dependent enzymes, and can be subdivided according to their structure and reaction mechanisms: type IIA (topoisomerase II or gyrase, and topoisomerase IV) and type IIB (topoisomerase VI). These enzymes are responsible for relaxing supercoiled DNA as well as for introducing both negative and positive supercoils [].Type IIA topoisomerases together manage chromosome integrity and topology in cells. Topoisomerase II (called gyrase in bacteria) primarily introduces negative supercoils into DNA. In bacteria, topoisomerase II consists of two polypeptide subunits, gyrA and gyrB, which form a heterotetramer: (BA)2. In most eukaryotes, topoisomerase II consists of a single polypeptide, where the N- and C-terminal regions correspond to gyrB and gyrA, respectively; this topoisomerase II forms a homodimer that is equivalent to the bacterial heterotetramer. There are four functional domains in topoisomerase II: domain 1 (N-terminal of gyrB) is an ATPase, domain 2 (C-terminal of gyrB) is responsible for subunit interactions (differs between eukaryotic and bacterial enzymes), domain 3 (N-terminal of gyrA) is responsible for the breaking-rejoining function through its capacity to form protein-DNA bridges, and domain 4 (C-terminal of gyrA) is able to non-specifically bind DNA [].Topoisomerase IV primarily decatenates DNA and relaxes positive supercoils, which is important in bacteria, where the circular chromosome becomes catenated, or linked, during replication []. Topoisomerase IV consists of two polypeptide subunits, parE and parC, where parC is homologous to gyrA and parE is homologous to gyrB.This entry represents the alpha-beta domain of subunit A (gyrA and parC) of bacterial gyrase and topoisomerase IV, and the equivalent C-terminal region in eukaryotic topoisomerase II composed of a single polypeptide.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

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6 Found In

Id Name Short Name Type
IPR002205 DNA topoisomerase, type IIA, subunit A/C-terminal Topo_IIA_A/C Domain
IPR013760 DNA topoisomerase, type IIA-like domain Topo_IIA_like_dom Domain
IPR001154 DNA topoisomerase II, eukaryotic-type TopoII_euk Family
IPR005743 DNA gyrase, subunit A GyrA Family
IPR005741 DNA topoisomerase IV subunit A, Gram-positive TopoIV_A_Gpos Family
IPR005742 DNA topoisomerase IV, subunit A, Gram-negative TopoIV_A_Gneg Family

0 Parent Features

7 Publications

First Author Title Year Journal Volume Pages
Roca J The mechanisms of DNA topoisomerases. 1995 Trends Biochem Sci 20 156-60
Champoux JJ DNA topoisomerases: structure, function, and mechanism. 2001 Annu Rev Biochem 70 369-413
Gadelle D Phylogenomics of type II DNA topoisomerases. 2003 Bioessays 25 232-42
Wang JC Cellular roles of DNA topoisomerases: a molecular perspective. 2002 Nat Rev Mol Cell Biol 3 430-40
Watt PM Structure and function of type II DNA topoisomerases. 1994 Biochem J 303 ( Pt 3) 681-95
Corbett KD The structural basis for substrate specificity in DNA topoisomerase IV. 2005 J Mol Biol 351 545-61
Huang WM Bacterial diversity based on type II DNA topoisomerase genes. 1996 Annu Rev Genet 30 79-107



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Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)