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J Biol Chem, Vol. 273, Issue 30, 19260-19268, July 24, 1998
From the The mammalian transcription factor LSF
(also known as CP2 and LBP-1c) binds as a homo-oligomer to directly
repeated elements in viral and cellular promoters. LSF and the
Drosophila transcription factor NTF-1 (also known as Elf-1
and Grainyhead) share a similar DNA binding region, which is unlike any
established DNA binding motifs. However, we demonstrate that dimeric
NTF-1 can bind an LSF half-site, whereas LSF cannot. To characterize
further the DNA binding and oligomerization characteristics of LSF,
truncation mutants were used to demonstrate that between 234 and 320 amino acids of LSF are required for high affinity DNA binding. Mixing of a truncation mutant with full-length LSF in a DNA binding assay established that the form of LSF that binds DNA is larger than a dimer.
Unexpectedly, one C-terminal deletion derivative, partially defective
in oligomerization properties, could occupy odd numbers of adjacent,
tandem LSF half-sites, unlike full-length LSF. The numbers of
DNA-protein complexes formed on multiple half-sites with this mutant
indicated that LSF binds DNA as a tetramer, although cross-linking
experiments confirmed a previous report concluding that LSF is
primarily dimeric in solution. The DNA binding and oligomerization
properties of LSF support models depicting novel mechanisms to prevent
continual, adjacent binding by a protein that recognizes directly
repeated DNA sequences.
LSF and NTF-1 Share a Conserved DNA Recognition Motif yet
Require Different Oligomerization States to Form a Stable Protein-DNA
Complex
and¶
Department of Microbiology and Molecular
Genetics,
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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