The interaction of Escherichia coli topoisomerase IV with DNA Journal Article

  


Authors: Peng, H.; Marians, K. J.
Article Title: The interaction of Escherichia coli topoisomerase IV with DNA
Abstract: The two type II topoisomerases in Escherichia coli, DNA gyrase and topoisomerase (Topo) IV, share considerable amino acid sequence similarity, yet they have distinctive topoisomerization activities. Only DNA gyrase can supercoil relaxed DNA, whereas during oriC DNA replication in vitro, only Topo IV can support the final stages of replication, processing of the late intermediate and decatenation of the daughter molecules. In order to develop an understanding for the basis of the differential activities of these two enzymes, we have initiated a characterization of Topo IV binding to DNA. We find that unlike gyrase, Topo IV neither constrains DNA in a positive supercoil when it binds nor protects a 150-base pair region of DNA from digestion with micrococcal nuclease. Consistent with this, DNase I footprinting experiments showed that Topo IV protected a 34-base pair region roughly centered about the topoisomerase-induced cleavage site. In addition, Topo IV preferentially bound supercoiled rather than relaxed DNA. Thus, the DNA binding characteristics of Topo IV are more akin to those of the type II eukaryotic enzymes rather than those of its prokaryotic partner.
Keywords: controlled study; nonhuman; dna replication; protein dna binding; dna; molecular sequence data; escherichia coli; base sequence; molecular interaction; dna topoisomerase (atp hydrolysing); dna binding; bacterial dna; dna topoisomerases, type ii; dna topoisomerase iv; dna topoisomerase; protein dna interaction; dna supercoiling; dna, superhelical; dna footprinting; deoxyribonuclease i; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.
Journal Title: Journal of Biological Chemistry
Volume: 270
Issue: 42
ISSN: 0021-9258
Publisher: American Society for Biochemistry and Molecular Biology  
Date Published: 1995-10-20
Start Page: 25286
End Page: 25290
Language: English
DOI: 10.1074/jbc.270.42.25286
PUBMED: 7559669
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028806614&doi=10.1074%2fjbc.270.42.25286&partnerID=40&md5=141d61bbbd75224fc0ebe2e640c9ade2
Notes: Article -- Export Date: 28 August 2018 -- Source: Scopus
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MSK Authors
  1. Kenneth Marians
    138 Marians
  2. Hong Peng
    9 Peng
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