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Volume 166, Issue 2

A highly processive actinobacterial topoisomerase I – thoughts on ’ demand for an enzyme with a unique C-terminal domain Open Access

Abstract

Topoisomerase I (TopA) is an essential enzyme that is required to remove excess negative supercoils from chromosomal DNA. Actinobacteria encode unusual TopA homologues with a unique C-terminal domain that contains lysine repeats and confers high enzyme processivity. Interestingly, the longest stretch of lysine repeats was identified in TopA from , environmental bacteria that undergo complex differentiation and produce a plethora of secondary metabolites. In this review, we aim to discuss potential advantages of the lysine repeats in TopA. We speculate that the chromosome organization, transcriptional regulation and lifestyle of these species demand a highly processive but also fine-tuneable relaxase. We hypothesize that the unique TopA provides flexible control of chromosomal topology and globally regulates gene expression.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): chromosome topology , Streptomyces and topoisomerase I
Funding
This study was supported by the:
  • Narodowym Centrum Nauki (Award 2014/15/NZ2/01067)
    • Principle Award Recipient: Dagmara Jakimowicz
  • Narodowe Centrum Nauki (Award 2016/22/NZ1/00122)
    • Principle Award Recipient: Marcin Jan Szafran
  • Narodowe Centrum Nauki (Award 2018/28/C/NZ1/00241)
    • Principle Award Recipient: Agnieszka Strzałka
© 2020 The Authors
  • This is an open-access article distributed under the terms of the Creative Commons Attribution License.
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2019-08-07
2024-05-07
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A highly processive actinobacterial topoisomerase I – thoughts on Streptomyces’ demand for an enzyme with a unique C-terminal domain
Microbiology 166, 120 (2020); https://doi.org/10.1099/mic.0.000841
/content/journal/micro/10.1099/mic.0.000841
/content/journal/micro/10.1099/mic.0.000841
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