Synergy of importin α recognition and DNA binding by the yeast transcriptional activator GAL4

Chee Kai Chan, David A. Jans

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The N-terminus of the yeast transcriptional activator GAL4 contains partially overlapping nuclear targeting and DNA binding functions. We have previously shown that GAL4 is recognised with high affinity by importin β and not by the conventional nuclear localisation sequence binding importin α subunit of the importin α/β heterodimer. The present study uses ELISA-based binding and electrophoretic mobility shift assays to show that recognition of GAL4 by importin α can occur, but only when GAL4 is bound to its specific DNA recognition sequence. Intriguingly, binding by importin α enhances DNA binding on the part of GAL4, implying a synergistic co-operation between these two functions. The results implicate a possible role for importin α in the nucleus additional to its established role in nuclear transport, as well as having implications for the use of GAL4 as a DNA carrier in gene therapy applications.

Original languageEnglish
Pages (from-to)221-224
Number of pages4
JournalFEBS Letters
Volume462
Issue number1-2
DOIs
Publication statusPublished - Nov 26 1999

Keywords

  • DNA binding protein
  • GAL4
  • Importin
  • Nuclear targeting signal
  • Transcription factor

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Synergy of importin α recognition and DNA binding by the yeast transcriptional activator GAL4'. Together they form a unique fingerprint.

  • Cite this