Abstract:
:In the brome mosaic virus (BMV) virion, the coat protein (CP) selectively contacts the RNA motifs that regulate translation and RNA replication (Hoover et al., 2016. J. Virol. 90, 7748). We hypothesize that the unstructured N-terminal arm (NTA) of the BMV CP can specifically recognize RNA motifs. Using ion mobility spectrometry-mass spectrometry, we demonstrate that peptides containing the NTA of the CP were found to preferentially bind to an RNA hairpin motif that directs the initiation of BMV RNA synthesis. RNA binding causes the peptide to change from heterogeneous structures to a single family of structures. Fluorescence anisotropy, fluorescence quenching and size exclusion chromatography experiments all confirm that the NTA can specific recognize the RNA motif. The peptide introduced into plants along with BMV virion increased accumulation of the BMV CP and accelerated the rate of minus-strand RNA synthesis. The intrinsically disordered BMV NTA could thus specifically recognize BMV RNAs to affect viral infection.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Jacobs A,Hoover H,Smith E,Clemmer DE,Kim CH,Kao CCdoi
10.1093/nar/gkx1087subject
Has Abstractpub_date
2018-01-09 00:00:00pages
324-335issue
1eissn
0305-1048issn
1362-4962pii
4616871journal_volume
46pub_type
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