Literature DB >> 20210704

Structure and mechanism of action of type IA DNA topoisomerases.

D V Bugreev1, G A Nevinsky.   

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.

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Year:  2009        PMID: 20210704     DOI: 10.1134/s0006297909130045

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  8 in total

Review 1.  The many lives of type IA topoisomerases.

Authors:  Anna H Bizard; Ian D Hickson
Journal:  J Biol Chem       Date:  2020-04-10       Impact factor: 5.157

2.  Topoisomerase I (TopA) is recruited to ParB complexes and is required for proper chromosome organization during Streptomyces coelicolor sporulation.

Authors:  Marcin Szafran; Patrycja Skut; Bartosz Ditkowski; Katarzyna Ginda; Govind Chandra; Jolanta Zakrzewska-Czerwińska; Dagmara Jakimowicz
Journal:  J Bacteriol       Date:  2013-08-02       Impact factor: 3.490

3.  Mechanistic insights from structure of Mycobacterium smegmatis topoisomerase I with ssDNA bound to both N- and C-terminal domains.

Authors:  Nan Cao; Kemin Tan; Xiaobing Zuo; Thirunavukkarasu Annamalai; Yuk-Ching Tse-Dinh
Journal:  Nucleic Acids Res       Date:  2020-05-07       Impact factor: 16.971

4.  Swapping of The N-Terminal Domain of Human Topoisomerase 1B with the Corresponding Plasmodium Falciparum Counterpart Strongly Impairs Enzyme Activity.

Authors:  Jagadish Babu Dasari; Bini Chhetri Soren; Alessio Ottaviani; Cinzia Tesauro; Simona Marino; Beatrice Messina; Paola Fiorani
Journal:  Rep Biochem Mol Biol       Date:  2020-01

5.  A highly processive actinobacterial topoisomerase I - thoughts on Streptomyces' demand for an enzyme with a unique C-terminal domain.

Authors:  Marcin J Szafran; Agnieszka Strzałka; Dagmara Jakimowicz
Journal:  Microbiology (Reading)       Date:  2019-08-07       Impact factor: 2.777

Review 6.  Recent developments in topoisomerase-targeted cancer chemotherapy.

Authors:  KirkE Hevener; Tatsiana A Verstak; Katie E Lutat; Daniel L Riggsbee; Jeremiah W Mooney
Journal:  Acta Pharm Sin B       Date:  2018-07-25       Impact factor: 11.413

7.  Direct regulation of topoisomerase activity by a nucleoid-associated protein.

Authors:  Soumitra Ghosh; Bratati Mallick; Valakunja Nagaraja
Journal:  Nucleic Acids Res       Date:  2014-09-08       Impact factor: 16.971

8.  C-terminal lysine repeats in Streptomyces topoisomerase I stabilize the enzyme-DNA complex and confer high enzyme processivity.

Authors:  Agnieszka Strzalka; Marcin J Szafran; Terence Strick; Dagmara Jakimowicz
Journal:  Nucleic Acids Res       Date:  2017-11-16       Impact factor: 16.971

  8 in total

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