Year: 2004
Type: dissertation
Abstract: helix protrusions from one monomer to another and shared hydrophobic space formed by helices stabilizes the interaction.The hydrophobic residues in the helices were absolutely crucial for the interaction.The interaction was also prerequisite for the N protein perinuclear localization in the cytoplasm.These data together with the visualization of N protein trimer after image reconstruction allowed us to suggest a model for the N protein oligomerization.The model shows that the N protein oligomerization is initiated by trimerization via coiled-coil motifs in the N-terminus and continued via helix protrusions in the C-terminus.The fourth aim was to search for cellular proteins interacting with the N protein.We found small ubiquitin-related modifier-1 (SUMO-1) interacting with the N protein in the close vicinity to nuclear membrane.Two amino acid stretches that included positively charged amino acids in SUMO-1 were found responsible for the interaction with the N protein.The SUMO-1 interaction may be needed for the N protein localization to the Golgi region.Like nucleoproteins of many negative-strand RNA viruses, hantavirus N protein is a multifunctional protein participating in various interactions during virus replication.Now that we can better understand the functional domains of the N protein, it provides us a good model to study different aspects of structure-function relationships in other bunyaviruses.
Source: Työväentutkimus Vuosikirja
Author: Pasi Kaukinen
Language: English
Topic: Viral Infections and Vectors
Subfield: Infectious Diseases
Field: Medicine
Domain: Health Sciences
Open Access status: green
OpenAlex ID: W2106836068