Virion tails of Beet yellows virus: Coordinated assembly by three structural proteins.
Filamentous virions of Beet yellows virus contain a long body formed by a major capsid protein and a short tail that is assembled by a minor capsid protein (CPm), an Hsp70-homolog (Hsp70h), a 64-kDa protein (p64), and a 20-kDa protein (p20). Using mutation analysis and newly developed in planta assays, here we investigate the genetic requirements for the tail assembly. We show that the inactivation of CPm dramatically reduces incorporation of both Hsp70h and p64. Furthermore, inactivation of Hsp70h prevents incorporation of p64 into virions and vice versa. Hsp70h and p64 are each required for efficient incorporation of CPm. We also show that the tails possessing normal relative amounts of CPm, Hsp70h, and p64 can be formed in the absence of the major capsid protein and p20. Similar to the tails isolated from the wild-type virions, these mutant tails encapsidate the approximately 700 nt-long, 5'-terminal segments of the viral RNA. Taken together, our results imply that CPm, Hsp70h and p64 act cooperatively to encapsidate a defined region of the closterovirus genome.
Alzhanova
Dina V
DV
Department of Botany and Plant Pathology and Center for Genome Research and Biocomputing, Oregon State University, Corvallis, OR 97331, USA.
Prokhnevsky
Alexey I
AI
Peremyslov
Valera V
VV
Dolja
Valerian V
VV
D001483:Base Sequence; D036022:Capsid Proteins / Q000378:metabolism*; D017790:Closterovirus / Q000235:genetics / Q000502:physiology*; D004252:DNA Mutational Analysis; D016679:Genome, Viral; D015151:Immunoblotting; D008969:Molecular Sequence Data; D016296:Mutagenesis; D012367:RNA, Viral / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D014026:Nicotiana / Q000821:virology; D017376:Viral Tail Proteins / Q000235:genetics / Q000378:metabolism*; D014771:Virion / Q000737:chemistry / Q000502:physiology*; D019065:Virus Assembly
D036022:Capsid Proteins; D012367:RNA, Viral; D017376:Viral Tail Proteins