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 language | English |
|---|---|
| Pages (from-to) | 221-224 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 462 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - Nov 26 1999 |
| Externally published | Yes |
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Keywords
- DNA binding protein
- GAL4
- Importin
- Nuclear targeting signal
- Transcription factor
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Synergy of importin α recognition and DNA binding by the yeast transcriptional activator GAL4. / Chan, Chee Kai; Jans, David A.
In: FEBS Letters, Vol. 462, No. 1-2, 26.11.1999, p. 221-224.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Synergy of importin α recognition and DNA binding by the yeast transcriptional activator GAL4
AU - Chan, Chee Kai
AU - Jans, David A.
PY - 1999/11/26
Y1 - 1999/11/26
N2 - 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.
AB - 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.
KW - DNA binding protein
KW - GAL4
KW - Importin
KW - Nuclear targeting signal
KW - Transcription factor
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U2 - 10.1016/S0014-5793(99)01515-X
DO - 10.1016/S0014-5793(99)01515-X
M3 - Article
VL - 462
SP - 221
EP - 224
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-2
ER -