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J Gen Virol. 2014 Oct;95(Pt 10):2321-7. doi: 10.1099/vir.0.066514-0. Epub 2014 Jun 17.

Evidence for lysine acetylation in the coat protein of a polerovirus.

Author information

1
USDA-Agricultural Research Service, Ithaca, NY 14853, USA Department of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY 14853, USA Boyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA mlc68@cornell.edu.
2
Department of Genome Sciences, University of Washington, Seattle, WA 98109, USA.
3
Boyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA.
4
USDA-Agricultural Research Service, Ithaca, NY 14853, USA Boyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA.
5
USDA-Agricultural Research Service, Ithaca, NY 14853, USA Department of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY 14853, USA.

Abstract

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.

PMID:
24939649
PMCID:
PMC4165934
DOI:
10.1099/vir.0.066514-0
[Indexed for MEDLINE]
Free PMC Article

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