PMID: 11918669Mar 29, 2002Paper

A GyrB-GyrA fusion protein expressed in yeast cells is able to remove DNA supercoils but cannot substitute eukaryotic topoisomerase II

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
Sonia Trigueros, Joaquim Roca

Abstract

Type II topoisomerases are a highly conserved class of enzymes which transport one double-stranded DNA segment through a transient break in another. Whereas the eukaryotic enzymes are homodimers of a single polypeptide, their bacterial homologues are homodimers of two independently coded protein subunits. Unlike eukaryotic topoisomerase II and bacterial topoisomerase IV, DNA gyrase is a bacterial type II topoisomerase which specializes in intramolecular DNA transport. We have fused the Escherichia coli coding sequences for the proteins GyrB and GyrA, which comprise DNA gyrase. This fusion was expressed in yeast cells and yielded the expected full-length protein product. When it was expressed in Deltatop1- top2-4 yeast cells, the fusion protein compensated their slow growth and reverted their elevated chromosomal excision of ribosomal genes. Furthermore, it removed DNA positive supercoils. The fusion protein, however, was unable to complement the temperature-dependent lethality of top2-4 cells. Fusion of the E. coli GyrB and GyrA proteins leads to a catalytically active topoisomerase which compensates several phenotypic traits attributed to unconstrained DNA supercoiling in topoisomerase-deficient cells. However, since the fusio...Continue Reading

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Citations

Jun 22, 2012·Nucleic Acids Research·Ricky S JoshiJoaquim Roca
Oct 9, 2007·Electrophoresis·María-Dolores Mayán-SantosJorge B Schvartzman
Dec 30, 2014·Médecine sciences : M/S·Julie PapillonValérie Lamour
Jul 19, 2002·Yeast
Sep 2, 2015·Antimicrobial Agents and Chemotherapy·Chunhui ChenDavid C Hooper
Aug 6, 2010·Nature·Benjamin D BaxMichael N Gwynn
Jan 25, 2018·The Biochemical Journal·Justine L DelgadoHiroshi Hiasa

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