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Synergy of importin α recognition and DNA binding by the yeast transcriptional activator GAL4
Author(s) -
Chan Chee-Kai,
Jans David A
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01515-x
Subject(s) - importin , nuclear transport , activator (genetics) , nuclear localization sequence , biology , microbiology and biotechnology , nuclear protein , dna , electrophoretic mobility shift assay , transcription factor , biochemistry , chemistry , cell nucleus , gene , nucleus
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.