Extension of the binding motif of the Sin3 interacting domain of the Mad family proteins. van Ingen, H., Lasonder, E., Jansen, J. F., Kaan, A. M., Spronk, C. A., Stunnenberg, H. G., & Vuister, G. W. Biochemistry, 43(1):46-54, 2004. van Ingen, Hugo Lasonder, Edwin Jansen, Jacobus F A Kaan, Anita M Spronk, Christian A E M Stunnenberg, Henk G Vuister, Geerten W eng Comparative Study Research Support, Non-U.S. Gov't 2004/01/07 05:00 Biochemistry. 2004 Jan 13;43(1):46-54. doi: 10.1021/bi0355645.![Extension of the binding motif of the Sin3 interacting domain of the Mad family proteins [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Sin3 forms the scaffold for a multiprotein corepressor complex that silences transcription via the action of histone deacetylases. Sin3 is recruited to the DNA by several DNA binding repressors, such as the helix-loop-helix proteins of the Mad family. Here, we elaborate on the Mad-Sin3 interaction based on a binding study, solution structure, and dynamics of the PAH2 domain of mSin3 in complex to an extended Sin3 interacting domain (SID) of 24 residues of Mad1. We show that SID residues Met7 and Glu23, outside the previously defined minimal binding motif, mediate additional hydrophobic and electrostatic interactions with PAH2. On the basis of these results we propose an extended consensus sequence describing the PAH2-SID interaction specifically for the Mad family, showing that residues outside the hydrophobic core of the SID interact with PAH2 and modulate binding affinity to appropriate levels.
@article{RN123,
author = {van Ingen, H. and Lasonder, E. and Jansen, J. F. and Kaan, A. M. and Spronk, C. A. and Stunnenberg, H. G. and Vuister, G. W.},
title = {Extension of the binding motif of the Sin3 interacting domain of the Mad family proteins},
journal = {Biochemistry},
volume = {43},
number = {1},
pages = {46-54},
note = {van Ingen, Hugo
Lasonder, Edwin
Jansen, Jacobus F A
Kaan, Anita M
Spronk, Christian A E M
Stunnenberg, Henk G
Vuister, Geerten W
eng
Comparative Study
Research Support, Non-U.S. Gov't
2004/01/07 05:00
Biochemistry. 2004 Jan 13;43(1):46-54. doi: 10.1021/bi0355645.},
abstract = {Sin3 forms the scaffold for a multiprotein corepressor complex that silences transcription via the action of histone deacetylases. Sin3 is recruited to the DNA by several DNA binding repressors, such as the helix-loop-helix proteins of the Mad family. Here, we elaborate on the Mad-Sin3 interaction based on a binding study, solution structure, and dynamics of the PAH2 domain of mSin3 in complex to an extended Sin3 interacting domain (SID) of 24 residues of Mad1. We show that SID residues Met7 and Glu23, outside the previously defined minimal binding motif, mediate additional hydrophobic and electrostatic interactions with PAH2. On the basis of these results we propose an extended consensus sequence describing the PAH2-SID interaction specifically for the Mad family, showing that residues outside the hydrophobic core of the SID interact with PAH2 and modulate binding affinity to appropriate levels.},
keywords = {Amino Acid Motifs
Amino Acid Sequence
Animals
Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
Caenorhabditis elegans Proteins/chemistry
Conserved Sequence
Crystallography, X-Ray
DNA-Binding Proteins/*chemistry
Fungal Proteins/chemistry
Histone Deacetylases
Humans
Membrane Proteins/chemistry
Molecular Sequence Data
Multigene Family
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Protein Structure, Tertiary
*Repressor Proteins
*Saccharomyces cerevisiae Proteins
Sequence Alignment
*Sequence Homology, Amino Acid
Solutions
Surface Plasmon Resonance
Thermodynamics
Transcription Factors/*chemistry},
ISSN = {0006-2960 (Print)
0006-2960 (Linking)},
DOI = {10.1021/bi0355645},
url = {http://www.ncbi.nlm.nih.gov/pubmed/14705930
https://pubs.acs.org/doi/10.1021/bi0355645},
year = {2004},
type = {Journal Article}
}
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