Effects of Nucleotide and End-Dependent Actin Conformations on Polymerization.

Actin Cytoskeleton / metabolism Actins / metabolism Adenosine Diphosphate Adenosine Triphosphate Kinetics Microfilament Proteins / metabolism Polymerization Protein Conformation

Journal

Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626

Informations de publication

Date de publication:
03 11 2020
Historique:
received: 11 03 2020
revised: 04 09 2020
accepted: 10 09 2020
pubmed: 21 10 2020
medline: 15 5 2021
entrez: 20 10 2020
Statut: ppublish

Résumé

The regulation of actin is key for controlled cellular function. Filaments are regulated by actin-binding proteins, but the nucleotide state of actin is also an important factor. From extended molecular dynamics simulations, we find that both nucleotide states of the actin monomer have significantly less twist than their crystal structures and that the ATP monomer is flatter than the ADP form. We also find that the filament's pointed end is flatter than the remainder of the filament and has a conformation distinct from G-actin, meaning that incoming monomers would need to undergo isomerization that would weaken the affinity and slow polymerization. Conversely, the barbed end of the filament takes on a conformation nearly identical to the ATP monomer, enhancing ATP G-actin's ability to polymerize as compared with ADP G-actin. The thermodynamic penalty imposed by differences in isomerization for the ATP and ADP growth at the barbed end exactly matches experimental results.

Identifiants

DOI: 10.1016/j.bpj.2020.09.024 PMID: 33080221 PMC: PMC7677244
pubmed: 33080221
pii: S0006-3495(20)30735-9
doi: 10.1016/j.bpj.2020.09.024
pmc: PMC7677244
pii:
doi:

Substances chimiques

Actins 0
Microfilament Proteins 0
Adenosine Diphosphate 61D2G4IYVH
Adenosine Triphosphate 8L70Q75FXE

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

1800-1810

Subventions

Organisme : NIGMS NIH HHS
ID : K12 GM111725
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM136822
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007499
Pays : United States

Informations de copyright

Copyright © 2020 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Auteurs

Lauren Jepsen (L)

Department of Biomedical Engineering and Center for Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan.

David Sept (D)

Department of Biomedical Engineering and Center for Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan. Electronic address: dsept@umich.edu.

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Classifications MeSH

questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Cytosquelette › Cytosquelette d'actine › Effects of Nucleotide and End-Dependent Actin...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Protéines des microfilaments › Actines › Effects of Nucleotide and End-Dependent Actin...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Ribonucléotides › Nucléotides adényliques › ADP › Effects of Nucleotide and End-Dependent Actin...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Nucléotides › Ribonucléotides › Nucléotides adényliques › Adénosine triphosphate › Effects of Nucleotide and End-Dependent Actin...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Cinétique › Effects of Nucleotide and End-Dependent Actin...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Protéines des microfilaments › Effects of Nucleotide and End-Dependent Actin...
questionsmedicales.fr › Phénomènes chimiques › Polymérisation › Effects of Nucleotide and End-Dependent Actin...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Effects of Nucleotide and End-Dependent Actin...