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• W92841738 abstract "The encapsidation process of tomato spotted wilt tospovirus (TSWV), a member of the Bunyaviridae family with a tripartite, ambisense RNA genome, was investigated. Encapsidation is the binding of many copies of the nucleocapsid protein N to the viral RNA in a well-ordered manner. It is known that other viruses of the same family encapsidate both genomic and antigenomic RNA but not viral mRNA or cellular RNAs. There are only few exceptions known. This work focuses on the molecular basis of this encapsidation specificity. Furthermore, the influence of the N protein oligomerization state on RNA binding is investigated by using N protein mutants with a decreased ability to form multimers. Both gel filtration and Blue Native electrophoresis experiments demonstrated that untagged wild type TSWV nucleocapsid protein N was mainly present as a high molecular weight complex. Tetrameric and trimeric complexes were also found, but hardly any dimers or monomers were present. These low molecular weight complexes may represent stable intermediate states in the encapsidation process. Biochemical analyses of point and deletion mutants of the N protein support the view of a homotypic “head-to-tail” interaction with an N-terminal and a C-terminal interaction domain. Secondary structure analyses using circular dichroism spectroscopy provide evidence for an involvement of α-helices in the protein – protein interaction. The results presented demonstrate the successful utility of Blue Native PAGE in analysing nucleocapsid protein oligomerization of a plant virus. Protein – RNA complexes were analysed in GEMSAs and filter binding assays. Compared to wildtype N protein, N protein mutants with a reduced ability to oligomerize showed an apparently higher RNA binding capability. In BN-PAGE and gel filtration studies, these mutants were present as monomers to a much higher degree than wild type N protein. This suggests that monomeric N protein interacts with RNA. Different N protein – RNA interactions were quantified and cooperativity was found in most cases, even for N protein mutants with a limited ability to oligomerize. A higher affinity of the N protein for sequences at the 5’ end of the genomic S RNA segment was found, as compared to the 3’ end and other viral and nonviral RNAs. The specifically recognized sequence resides within a 39-nucleotide stretch at the 5’ terminal end. This observation is in agreement with recent studies of members of the closely related Hantavirus and Bunyavirus genera. Therefore, the 5’ terminal sequence may represent a conserved origin of assembly within the Bunyaviridae family. Although this sequence is part of both the genomic S RNA and the NSsmRNA, the host-derived 5’ terminal cap structure of viral mRNAs may alter the secondary structure of the proposed origin of assembly such that only genomic S RNAs are recognized by the N protein. Based on these results, a model describing the molecular events during encapsidation as well as an N protein-mediated switch from transcription to replication is discussed." @default.
• W92841738 created "2016-06-24" @default.
• W92841738 creator A5032994868 @default.
• W92841738 date "2002-01-01" @default.
• W92841738 modified "2023-09-27" @default.
• W92841738 title "Molekulare Charakterisierung des Nukleokapsidaufbaus von TSWV (Tomato Spotted Wilt Virus)" @default.
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