Hinge like domain motion facilitates human RBMS1 protein binding to proto-oncogene c-myc promoter.
Binding Sites
Calorimetry, Differential Scanning
Crystallography, X-Ray
DNA-Binding Proteins
/ chemistry
Gene Expression
Genes, myc
Humans
Magnetic Resonance Spectroscopy
Molecular Dynamics Simulation
Mutagenesis, Site-Directed
Promoter Regions, Genetic
Protein Binding
Protein Domains
Proto-Oncogene Mas
Proto-Oncogene Proteins c-myc
/ chemistry
RNA-Binding Proteins
/ chemistry
Recombinant Proteins
Thermodynamics
Journal
Nucleic acids research
ISSN: 1362-4962
Titre abrégé: Nucleic Acids Res
Pays: England
ID NLM: 0411011
Informations de publication
Date de publication:
04 06 2021
04 06 2021
Historique:
accepted:
24
04
2021
revised:
02
04
2021
received:
08
10
2020
pubmed:
18
5
2021
medline:
29
6
2021
entrez:
17
5
2021
Statut:
ppublish
Résumé
DNA binding proteins recognize DNA specifically or non-specifically using direct and indirect readout mechanisms like sliding, hopping, and diffusion. However, a common difficulty in explicitly elucidating any particular mechanism of site-specific DNA-protein recognition is the lack of knowledge regarding target sequences and inadequate account of non-specific interactions, in general. Here, we decipher the structural basis of target search performed by the key regulator of expression of c-myc proto-oncogene, the human RBMS1 protein. In this study, we have shown the structural reorganization of this multi-domain protein required for recognizing the specific c-myc promoter sequence. The results suggest that a synergy between structural re-organization and thermodynamics is necessary for the recognition of target sequences. The study presents another perspective of looking at the DNA-protein interactions.
Identifiants
pubmed: 33999211
pii: 6276930
doi: 10.1093/nar/gkab363
pmc: PMC8191779
doi:
Substances chimiques
DNA-Binding Proteins
0
MAS1 protein, human
0
Proto-Oncogene Mas
0
Proto-Oncogene Proteins c-myc
0
RBMS1 protein, human
0
RNA-Binding Proteins
0
Recombinant Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
5943-5955Informations de copyright
© The Author(s) 2021. Published by Oxford University Press on behalf of Nucleic Acids Research.
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