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Nuclear-localization of bacterial Streptoalloteichus-hindustanus bleomycin resistance protein in mammalian-cells

Academic Article
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Overview

authors

  • Calmels, T. P. G.
  • Mistry, J. S.
  • Watkins, S. C.
  • Robbins, Paul D.
  • McGuire, R.
  • Lazo, J. S.

publication date

  • December 1993

journal

  • Molecular Pharmacology  Journal

abstract

  • Prokaryotes produce a variety of toxins that affect genomic function of both eukaryotes and prokaryotes. The 375-base pair bacterial gene Streptoalloteichus hindustanus (Sh) ble encodes a small protein, Streptoalloteichus hindustanus bleomycin resistance protein (BRP), that inhibits in vitro DNA cleavage by the prokaryotic glycopeptide bleomycin, which is a clinically used anticancer drug. NIH/3T3 cells infected with a retroviral vector containing Sh ble (SH-9 cells) were highly resistant to the cytotoxicity of bleomycin-like drugs but not to the cytotoxicity of other, structurally unrelated, DNA-cleaving agents. Expression of BRP did not markedly alter total cellular content or distribution of bleomycin-like compounds. Fluorescently labeled bleomycin was primarily localized in cytoplasmic vesicles in NIH/3T3 and SH-9 cells, whereas BRP, which has no established nuclear localization sequence, was segregated to the nucleus and more specifically to euchromatin. This karyophilic BRP may intercept bleomycin in the nucleus.

subject areas

  • 3T3 Cells
  • Actinomycetales
  • Animals
  • Bacterial Proteins
  • Bleomycin
  • Blotting, Western
  • Cell Nucleus
  • DNA Damage
  • Drug Resistance, Microbial
  • Immunohistochemistry
  • Mice
  • Microscopy, Immunoelectron
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Identity

International Standard Serial Number (ISSN)

  • 0026-895X

PubMed ID

  • 7505390
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Additional Document Info

start page

  • 1135

end page

  • 1141

volume

  • 44

issue

  • 6

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