Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

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.

In: Journal of Biological Chemistry, Vol. 275, No. 35, 01.09.2000, p. 27266-73.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

van Beest, M, Dooijes, D, van De Wetering, M, Kjaerulff, S, Bonvin, A, Nielsen, O, Clevers, H & Nielsen, O 2000, 'Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs', Journal of Biological Chemistry, vol. 275, no. 35, pp. 27266-73. https://doi.org/10.1074/jbc.M004102200

APA

van Beest, M., Dooijes, D., van De Wetering, M., Kjaerulff, S., Bonvin, A., Nielsen, O., Clevers, H., & Nielsen, O. (2000). Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs. Journal of Biological Chemistry, 275(35), 27266-73. https://doi.org/10.1074/jbc.M004102200

Vancouver

van Beest M, Dooijes D, van De Wetering M, Kjaerulff S, Bonvin A, Nielsen O et al. Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs. Journal of Biological Chemistry. 2000 Sep 1;275(35):27266-73. https://doi.org/10.1074/jbc.M004102200

Author

van Beest, M ; Dooijes, D ; van De Wetering, M ; Kjaerulff, S ; Bonvin, A ; Nielsen, O ; Clevers, H ; Nielsen, Olaf. / Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs. In: Journal of Biological Chemistry. 2000 ; Vol. 275, No. 35. pp. 27266-73.

Bibtex

@article{0e95f68bde4643fb963e42e2fe4e4a01,
title = "Sequence-specific high mobility group box factors recognize 10-12-base pair minor groove motifs",
abstract = "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.",
keywords = "Amino Acid Sequence, Base Sequence, Binding Sites, DNA, DNA Footprinting, DNA Methylation, Fungal Proteins, High Mobility Group Proteins, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Protein Conformation, Schizosaccharomyces pombe Proteins, Sequence Homology, Amino Acid, Transcription Factors",
author = "{van Beest}, M and D Dooijes and {van De Wetering}, M and S Kjaerulff and A Bonvin and O Nielsen and H Clevers and Olaf Nielsen",
year = "2000",
month = sep,
day = "1",
doi = "10.1074/jbc.M004102200",
language = "English",
volume = "275",
pages = "27266--73",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "35",

}

RIS

TY - JOUR

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