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Title: Structural basis for suppression of hypernegative DNA supercoiling by E. coli topoisomerase I

Journal Article · · Nucleic Acids Research
DOI:https://doi.org/10.1093/nar/gkv1073· OSTI ID:1261152
 [1];  [2];  [3];  [3];  [1];  [4]
  1. Argonne National Lab. (ANL), Argonne, IL (United States)
  2. Florida Intl Univ., Miami, FL (United States). Dept. of Chemistry and Biochemistry
  3. New York Medical College, Valhalla, NY (United States)
  4. Florida Intl Univ., Miami, FL (United States). Dept. of Chemistry and Biochemistry; Florida Intl Univ., Miami, FL (United States). Biomolecular Sciences Inst.

Escherichia coli topoisomerase I has an essential function in preventing hypernegative supercoiling of DNA. A full length structure of E. coli topoisomerase I reported here shows how the C-terminal domains bind single-stranded DNA (ssDNA) to recognize the accumulation of negative supercoils in duplex DNA. These C-terminal domains of E. coli topoisomerase I are known to interact with RNA polymerase, and two flexible linkers within the C-terminal domains may assist in the movement of the ssDNA for the rapid removal of transcription driven negative supercoils. The structure has also unveiled for the first time how the 4-Cys zinc ribbon domain and zinc ribbon-like domain bind ssDNA with primarily π -stacking interactions. Finally, this novel structure, in combination with new biochemical data, provides important insights into the mechanism of genome regulation by type IA topoisomerases that is essential for life, as well as the structures of homologous type IA TOP3α and TOP3β from higher eukaryotes that also have multiple 4-Cys zinc ribbon domains required for their physiological functions.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
USDOE; National Institutes of Health (NIH)
Grant/Contract Number:
AC02- 06CH11357; GM054226; GM094585
OSTI ID:
1261152
Journal Information:
Nucleic Acids Research, Vol. 43, Issue 22; ISSN 0305-1048
Publisher:
Oxford University PressCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 40 works
Citation information provided by
Web of Science

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Cited By (12)

Deacetylation of topoisomerase I is an important physiological function of E. coli CobB journal April 2017
Topoisomerase IV can functionally replace all type 1A topoisomerases in Bacillus subtilis journal April 2019
Probing hyper-negatively supercoiled mini-circles with nucleases and DNA binding proteins journal August 2018
Structural basis of the interaction between Topoisomerase IIIβ and the TDRD3 auxiliary factor journal February 2017
The topoisomerase 3α zinc-finger domain T1 of Arabidopsis thaliana is required for targeting the enzyme activity to Holliday junction-like DNA repair intermediates journal September 2018
The topoisomerase 3α zinc-finger domain T1 of Arabidopsis thaliana is required for targeting the enzyme activity to Holliday junction-like DNA repair intermediates text January 2018
A highly processive actinobacterial topoisomerase I – thoughts on Streptomyces’ demand for an enzyme with a unique C-terminal domain journal February 2020
Topoisomerases I and III inhibit R-loop formation to prevent unregulated replication in the chromosomal Ter region of Escherichia coli journal September 2018
Mechanism of Type IA Topoisomerases journal October 2020
Microbial Type IA Topoisomerase C-Terminal Domain Sequence Motifs, Distribution and Combination journal August 2022
RNA topoisomerase is prevalent in all domains of life and associates with polyribosomes in animals journal June 2016
Microheterogeneity of Topoisomerase IA/IB and Their DNA-Bound States journal February 2019

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