DNA-segment-capture model for loop extrusion by structural maintenance of chromosome (SMC) protein complexes.
Détails
Télécharger: 31175837_BIB_B273DE7A00DB.pdf (1664.74 [Ko])
Etat: Public
Version: Final published version
Licence: CC BY-NC 4.0
Etat: Public
Version: Final published version
Licence: CC BY-NC 4.0
ID Serval
serval:BIB_B273DE7A00DB
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
DNA-segment-capture model for loop extrusion by structural maintenance of chromosome (SMC) protein complexes.
Périodique
Nucleic acids research
ISSN
1362-4962 (Electronic)
ISSN-L
0305-1048
Statut éditorial
Publié
Date de publication
26/07/2019
Peer-reviewed
Oui
Volume
47
Numéro
13
Pages
6956-6972
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
Résumé
Cells possess remarkable control of the folding and entanglement topology of long and flexible chromosomal DNA molecules. It is thought that structural maintenance of chromosome (SMC) protein complexes play a crucial role in this, by organizing long DNAs into series of loops. Experimental data suggest that SMC complexes are able to translocate on DNA, as well as pull out lengths of DNA via a 'loop extrusion' process. We describe a Brownian loop-capture-ratchet model for translocation and loop extrusion based on known structural, catalytic, and DNA-binding properties of the Bacillus subtilis SMC complex. Our model provides an example of a new class of molecular motor where large conformational fluctuations of the motor 'track'-in this case DNA-are involved in the basic translocation process. Quantitative analysis of our model leads to a series of predictions for the motor properties of SMC complexes, most strikingly a strong dependence of SMC translocation velocity and step size on tension in the DNA track that it is moving along, with 'stalling' occuring at subpiconewton tensions. We discuss how the same mechanism might be used by structurally related SMC complexes (Escherichia coli MukBEF and eukaryote condensin, cohesin and SMC5/6) to organize genomic DNA.
Mots-clé
Adenosine Diphosphate/metabolism, Adenosine Triphosphate/metabolism, Animals, Bacterial Proteins/metabolism, Cell Cycle Proteins/metabolism, Chromosomal Proteins, Non-Histone/metabolism, DNA/chemistry, DNA/metabolism, Eukaryotic Cells/metabolism, Kinetics, Models, Chemical, Molecular Motor Proteins/metabolism, Multiprotein Complexes/metabolism, Nucleic Acid Conformation, Protein Binding, Protein Conformation, Stress, Mechanical, Thermodynamics
Pubmed
Web of science
Open Access
Oui
Création de la notice
17/06/2019 21:47
Dernière modification de la notice
15/01/2021 7:11