DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK Journal Article


Authors: Bigot, S.; Marians, K. J.
Article Title: DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK
Abstract: We have studied the stimulation of topoisomerase IV (Topo IV) by the C-terminal AAA+ domain of FtsK. These two proteins combine to assure proper chromosome segregation in the cell. Stimulation of Topo IV activity was dependent on the chirality of the DNA substrate: FtsK stimulated decatenation of catenated DNA and relaxation of positively supercoiled [(+)ve sc] DNA, but inhibited relaxation of negatively supercoiled [(-)ve sc] DNA. The DNA translocation activity of FtsK was not required for stimulation, but was required for inhibition. DNA chirality did not affect any of the activities of FtsK, suggesting that FtsK possesses an inherent Topo IV stimulatory activity that is presumably mediated by protein-protein interactions, the stability of Topo IV on the DNA substrate dictated the effect observed. Inhibition occurs because FtsK can strip distributively acting topoisomerase off (-)ve scDNA, but not from either (+)ve scDNA or catenated DNA where the enzyme acts processively. Our analyses suggest that FtsK increases the efficiency of trapping of the transfer segment of DNA during the catalytic cycle of the topoisomerase. © The Author(s) 2010.
Keywords: controlled study; unclassified drug; protein domain; protein function; protein analysis; metabolism; carboxy terminal sequence; protein protein interaction; cell protein; membrane proteins; in vitro study; enzyme activity; chemistry; dna; enzyme regulation; membrane protein; protein structure, tertiary; protein tertiary structure; dna topoisomerase iv; chromosome segregation; escherichia coli proteins; ftsk protein; catenated dna; escherichia coli protein; ftsk protein, e coli; chirality; dna supercoiling; enzyme stability; dna, catenated; dna, superhelical
Journal Title: Nucleic Acids Research
Volume: 38
Issue: 9
ISSN: 0305-1048
Publisher: Oxford University Press  
Date Published: 2010-05-01
Start Page: 3031
End Page: 3040
Language: English
DOI: 10.1093/nar/gkp1243
PUBMED: 20081205
PROVIDER: scopus
PMCID: PMC2875013
DOI/URL:
Notes: --- - "Export Date: 20 April 2011" - "Art. No.: gkp1243" - "CODEN: NARHA" - "Source: Scopus"
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  1. Sarah Juliette Bigot
    1 Bigot
  2. Kenneth Marians
    138 Marians