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Papers In Press, published online ahead of print February 7, 2002
Molecular Cell Biology, The Rockefeller University, New York, NY 10021
Corresponding Author: yange{at}rockvax.rockefeller.edu
The STAT1 transcription factor is organized into several highly conserved domains, each of which has been assigned a function with the exception of the linker domain. We previously characterized a mutant in the linker domain of STAT1 which gave normal DNA binding using a standard probe in an electrophoretic mobility assay but failed to activate transcription in response to IFNg. We now report the mechanistic basis for the inactivity of this STAT1(KE544-545AA) mutant. Rather than failing to attract transcriptional coactivators, the STAT1(KE544-545AA) mutant has a subtle biophysical defect which prevents accumulation of the activated protein on chromatin in vivo: the mutant has comparable Kd with greatly increased koff for DNA binding. The increase in both on rate and off rate of DNA binding results in a substantially reduced residence time of STAT1(KE544-545AA) on STAT binding sites. We find a similar correlation between off-rate and transcriptional potency for STAT1(N460A) which bears a mutation in the DNA binding domain. These results yield insight into the rate of complex assembly involving STAT1 that leads to transcriptional stimulation.
J. Biol. Chem, 10.1074/jbc.M112038200
Submitted on December 18, 2001
Revised on February 7, 2002
Accepted on February 7, 2002
Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant
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