Article ; Online: Cryo-EM of the Nucleosome Core Particle Bound to Ran-RCC1 Reveals a Dynamic Complex.
2024 Volume 63, Issue 7, Page(s) 880–892
Abstract: Ras-related nuclear protein (Ran) is a member of the Ras superfamily of small guanosine triphosphatases (GTPases) and a regulator of multiple cellular processes. In healthy cells, the GTP-bound form of Ran is concentrated at chromatin, creating a Ran•GTP ...
Abstract | Ras-related nuclear protein (Ran) is a member of the Ras superfamily of small guanosine triphosphatases (GTPases) and a regulator of multiple cellular processes. In healthy cells, the GTP-bound form of Ran is concentrated at chromatin, creating a Ran•GTP gradient that provides the driving force for nucleocytoplasmic transport, mitotic spindle assembly, and nuclear envelope formation. The Ran•GTP gradient is maintained by the regulator of chromatin condensation 1 (RCC1), a guanine nucleotide exchange factor that accelerates GDP/GTP exchange in Ran. RCC1 interacts with nucleosomes, which are the fundamental repeating units of eukaryotic chromatin. Here, we present a cryo-EM analysis of a trimeric complex composed of the nucleosome core particle (NCP), RCC1, and Ran. While the contacts between RCC1 and Ran in the complex are preserved compared with a previously determined structure of RCC1-Ran, our study reveals that RCC1 and Ran interact dynamically with the NCP and undergo rocking motions on the nucleosome surface. Furthermore, the switch 1 region of Ran, which plays an important role in mediating conformational changes associated with the substitution of GDP and GTP nucleotides in Ras family members, appears to undergo disorder-order transitions and forms transient contacts with the C-terminal helix of histone H2B. Nucleotide exchange assays performed in the presence and absence of NCPs are not consistent with an active role for nucleosomes in nucleotide exchange, at least |
---|---|
MeSH term(s) | Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Chromatin ; Cryoelectron Microscopy ; Guanosine Triphosphate/metabolism ; Nuclear Proteins/chemistry ; Nuclear Proteins/metabolism ; Nucleosomes/chemistry ; Nucleosomes/metabolism ; Nucleotides/metabolism ; ran GTP-Binding Protein/metabolism ; Humans ; Guanine Nucleotide Exchange Factors/chemistry ; Guanine Nucleotide Exchange Factors/metabolism |
Chemical Substances | Cell Cycle Proteins ; Chromatin ; Guanosine Triphosphate (86-01-1) ; Nuclear Proteins ; Nucleosomes ; Nucleotides ; ran GTP-Binding Protein (EC 3.6.5.2) ; RCC1 protein, human ; Guanine Nucleotide Exchange Factors |
Language | English |
Publishing date | 2024-03-19 |
Publishing country | United States |
Document type | Journal Article |
ZDB-ID | 1108-3 |
ISSN | 1520-4995 ; 0006-2960 |
ISSN (online) | 1520-4995 |
ISSN | 0006-2960 |
DOI | 10.1021/acs.biochem.3c00724 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
More links
Kategorien
In stock of ZB MED Cologne/Königswinter
Zs.A 217: Show issues | Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG) |
Order via subito
This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.