ArticleRNA (New York, N.Y.)2009
Investigating the specificity and stoichiometry of RNA binding by the nucleocapsid protein of Bunyamwera virus.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- The bipartite promoter ofJournal of virology · 2023Article
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- Mutagenic Analysis of Hazara Nairovirus Nontranslated Regions during Single- and Multistep Growth Identifies both Attenuating and Functionally Critical Sequences for Virus Replication.Journal of virology · 2020Article
- Article
- Structure and function analysis of nucleocapsid protein of tomato spotted wilt virus interacting with RNA using homology modeling.The Journal of biological chemistry · 2015Article
- The molecular biology of nairoviruses, an emerging group of tick-borne arboviruses.Archives of virology · 2014Review
- Probing bunyavirus N protein oligomerisation using mass spectrometry.Rapid communications in mass spectrometry : RCM · 2014Article
- Nucleocapsid protein structures from orthobunyaviruses reveal insight into ribonucleoprotein architecture and RNA polymerization.Nucleic acids research · 2013Article
- Bunyamwera virus possesses a distinct nucleocapsid protein to facilitate genome encapsidation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structure of the Leanyer orthobunyavirus nucleoprotein-RNA complex reveals unique architecture for RNA encapsidation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Structural basis for encapsidation of genomic RNA by La Crosse Orthobunyavirus nucleoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A versatile building block: the structures and functions of negative-sense single-stranded RNA virus nucleocapsid proteins.Protein & cell · 2012Review
- Expression, purification and crystallization of the Crimean-Congo haemorrhagic fever virus nucleocapsid protein.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyaviruses.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Critical epitopes in the nucleocapsid protein of SFTS virus recognized by a panel of SFTS patients derived human monoclonal antibodies.PloS one · 2012Article
- Investigations on the RNA binding and phosphorylation of groundnut bud necrosis virus nucleocapsid protein.Archives of virology · 2011Article
- Epidemiology and mutational analysis of global strains of Crimean-Congo haemorrhagic fever virus.Virologica Sinica · 2011Article
- Amino acid changes within the Bunyamwera virus nucleocapsid protein differentially affect the mRNA transcription and RNA replication activities of assembled ribonucleoprotein templates.The Journal of general virology · 2011Article
- Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Rift valley fever virus L protein forms a biologically active oligomer.Journal of virology · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Bunyamwera virus (BUNV) is the prototypic member of both the Orthobunyavirus genus and the Bunyaviridae family of negative stranded RNA viruses. In common with all negative stranded RNA viruses, the BUNV genomic and anti-genomic strands are not naked RNAs, but instead are encapsidated along their entire lengths with the virus-encoded nucleocapsid (N) protein to form a ribonucleoprotein (RNP) complex. This association is critical for the negative strand RNA virus life cycle because only RNPs are active for productive RNA synthesis and RNA packaging. We are interested in understanding the molecular details of how N and RNA components associate within the bunyavirus RNP, and what governs the apparently selective encapsidation of viral replication products. Toward this goal, we recently devised a protocol that allowed generation of native BUNV N protein that maintained solubility under physiological conditions and allowed formation of crystals that yielded high-resolution x-ray diffraction data. Here we extend this work to show that this soluble N protein is able to oligomerize and bind RNA to form a highly uniform RNP complex, which exhibits characteristics in common with the viral RNP. By extracting and sequencing RNAs bound to these model RNPs, we determined the stoichiometry of N-RNA association to be approximately 12 nucleotides per N monomer. In addition, we defined the minimal sequence requirement for BUNV RNA replication. By comparing this minimal sequence to those bound to our model RNP, we conclude that N protein does not obligatorily require a sequence or structure for RNA encapsidation.
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