Journal
JOURNAL OF GENERAL VIROLOGY
Volume 95, Issue -, Pages 2321-2327Publisher
MICROBIOLOGY SOC
DOI: 10.1099/vir.0.066514-0
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Funding
- USDA NIFA [1907-22000-021-20]
- NSF BREAD [1109989]
- Boyce Thompson Institute
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [1109989] Funding Source: National Science Foundation
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Virions of the RPV strain of Cereal yellow dwarf virus-RPV were purified from infected oat tissue and analysed by MS. Two conserved residues, K147 and K181, in the virus coat protein, were confidently identified to contain epsilon-N-acetyl groups. While no functional data are available for K147, K181 lies within an interfacial region critical for virion assembly and stability. The signature immonium ion at m/z 126.0919 demonstrated the presence of N-acetyllysine, and the sequence fragment ions enabled an unambiguous assignment of the epsilon-N-acetyl modification on K181. We hypothesize that selection favours acetylation of K181 in a fraction of coat protein monomers to stabilize the capsid by promoting intermonomer salt bridge formation.
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