Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs
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Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs. / van Beest, M; Dooijes, D; van De Wetering, M; Kjaerulff, S; Bonvin, A; Nielsen, O; Clevers, H; Nielsen, Olaf.
I: Journal of Biological Chemistry, Bind 275, Nr. 35, 01.09.2000, s. 27266-73.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs
AU - van Beest, M
AU - Dooijes, D
AU - van De Wetering, M
AU - Kjaerulff, S
AU - Bonvin, A
AU - Nielsen, O
AU - Clevers, H
AU - Nielsen, Olaf
PY - 2000/9/1
Y1 - 2000/9/1
N2 - Sequence-specific high mobility group (HMG) box factors bind and bend DNA via interactions in the minor groove. Three-dimensional NMR analyses have provided the structural basis for this interaction. The cognate HMG domain DNA motif is generally believed to span 6-8 bases. However, alignment of promoter elements controlled by the yeast genes ste11 and Rox1 has indicated strict conservation of a larger DNA motif. By site selection, we identify a highly specific 12-base pair motif for Ste11, AGAACAAAGAAA. Similarly, we show that Tcf1, MatMc, and Sox4 bind unique, highly specific DNA motifs of 12, 12, and 10 base pairs, respectively. Footprinting with a deletion mutant of Ste11 reveals a novel interaction between the 3' base pairs of the extended DNA motif and amino acids C-terminal to the HMG domain. The sequence-specific interaction of Ste11 with these 3' base pairs contributes significantly to binding and bending of the DNA motif.
AB - Sequence-specific high mobility group (HMG) box factors bind and bend DNA via interactions in the minor groove. Three-dimensional NMR analyses have provided the structural basis for this interaction. The cognate HMG domain DNA motif is generally believed to span 6-8 bases. However, alignment of promoter elements controlled by the yeast genes ste11 and Rox1 has indicated strict conservation of a larger DNA motif. By site selection, we identify a highly specific 12-base pair motif for Ste11, AGAACAAAGAAA. Similarly, we show that Tcf1, MatMc, and Sox4 bind unique, highly specific DNA motifs of 12, 12, and 10 base pairs, respectively. Footprinting with a deletion mutant of Ste11 reveals a novel interaction between the 3' base pairs of the extended DNA motif and amino acids C-terminal to the HMG domain. The sequence-specific interaction of Ste11 with these 3' base pairs contributes significantly to binding and bending of the DNA motif.
KW - Amino Acid Sequence
KW - Base Sequence
KW - Binding Sites
KW - DNA
KW - DNA Footprinting
KW - DNA Methylation
KW - Fungal Proteins
KW - High Mobility Group Proteins
KW - Magnetic Resonance Spectroscopy
KW - Models, Molecular
KW - Molecular Sequence Data
KW - Protein Conformation
KW - Schizosaccharomyces pombe Proteins
KW - Sequence Homology, Amino Acid
KW - Transcription Factors
U2 - 10.1074/jbc.M004102200
DO - 10.1074/jbc.M004102200
M3 - Journal article
C2 - 10867006
VL - 275
SP - 27266
EP - 27273
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 35
ER -
ID: 33576832