Synergy of importin α recognition and DNA binding by the yeast transcriptional activator GAL4
- 22 November 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 462 (1-2) , 221-224
- https://doi.org/10.1016/s0014-5793(99)01515-x
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 beta and not by the conventional nuclear localisation sequence binding importin alpha subunit of the importin alpha/beta heterodimer. The present study uses ELISA-based binding and electrophoretic mobility shift assays to show that recognition of GAL4 by importin alpha can occur, but only when GAL4 is bound to its specific DNA recognition sequence. Intriguingly, binding by importin alpha 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 alpha 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.Keywords
This publication has 28 references indexed in Scilit:
- Plant Importin α Binds Nuclear Localization Sequences with High Affinity and Can Mediate Nuclear Import Independent of Importin βJournal of Biological Chemistry, 1999
- Enhancement of Polylysine-Mediated Transferrinfection by Nuclear Localization Sequences: Polylysine Does Not Function as a Nuclear Localization SequenceHuman Gene Therapy, 1999
- Efficiency of Importin α/β-Mediated Nuclear Localization Sequence Recognition and Nuclear ImportPublished by Elsevier ,1999
- Mutual exclusivity of DNA binding and nuclear localization signal recognition by the yeast transcription factor GAL4: implications for nonviral DNA deliveryGene Therapy, 1998
- Nuclear Targeting of Chlorin e6 Enhances Its Photosensitizing ActivityJournal of Biological Chemistry, 1997
- Gene Transfer Using a Novel Fusion Protein, GAL4/InvasinHuman Gene Therapy, 1997
- Target Cell-specific DNA Transfer Mediated by a Chimeric Multidomain ProteinJournal of Biological Chemistry, 1996
- Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporinsCell, 1995
- Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor [published erratum appears in J Cell Biol 1994 Jan;124(1-2):217]The Journal of cell biology, 1993
- An amino-terminal fragment of GAL4 binds DNA as a dimerJournal of Molecular Biology, 1989