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A highly processive actinobacterial topoisomerase I - thoughts on Streptomyces' demand for an enzyme with a unique C-terminal domain.
Szafran, Marcin J; Strzalka, Agnieszka; Jakimowicz, Dagmara.
Afiliação
  • Szafran MJ; Laboratory of Molecular Microbiology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
  • Strzalka A; Laboratory of Molecular Microbiology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
  • Jakimowicz D; Laboratory of Molecular Microbiology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Microbiology (Reading) ; 166(2): 120-128, 2020 02.
Article em En | MEDLINE | ID: mdl-31390324
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 Streptomyces, 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 Streptomyces 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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Streptomyces / Proteínas de Bactérias / DNA Topoisomerases Tipo I Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Streptomyces / Proteínas de Bactérias / DNA Topoisomerases Tipo I Idioma: En Ano de publicação: 2020 Tipo de documento: Article