A plant viral coat protein RNA binding consensus sequence contains a crucial arginine.
A defining feature of alfalfa mosaic virus (AMV) and ilarviruses [type virus: tobacco streak virus (TSV)] is that, in addition to genomic RNAs, viral coat protein is required to establish infection in plants. AMV and TSV coat proteins, which share little primary amino acid sequence identity, are functionally interchangeable in RNA binding and initiation of infection. The lysine-rich amino-terminal RNA binding domain of the AMV coat protein lacks previously identified RNA binding motifs. Here, the AMV coat protein RNA binding domain is shown to contain a single arginine whose specific side chain and position are crucial for RNA binding. In addition, the putative RNA binding domain of two ilarvirus coat proteins, TSV and citrus variegation virus, is identified and also shown to contain a crucial arginine. AMV and ilarvirus coat protein sequence alignment centering on the key arginine revealed a new RNA binding consensus sequence. This consensus may explain in part why heterologous viral RNA-coat protein mixtures are infectious.
Harvard-MIT Division of Health Sciences and Technology, Massachusetts Institute of Technology, Cambridge 02139, USA.
P
P
Ansel-McKinney
S W
SW
Scott
M
M
Swanson
X
X
Ge
L
L
Gehrke
D017794:Alfalfa mosaic virus / Q000235:genetics; D000595:Amino Acid Sequence; D001120:Arginine; D001483:Base Sequence; D002213:Capsid / Q000737:chemistry* / Q000378:metabolism; D036022:Capsid Proteins; D016384:Consensus Sequence; D004722:Endoribonucleases / Q000378:metabolism; D019179:Ilarvirus / Q000235:genetics; D008969:Molecular Sequence Data; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry*
D036022:Capsid Proteins; D016601:RNA-Binding Proteins; C095691:coat protein, Alfalfa mosaic virus; C087151:RNA 3 coat protein, prune dwarf ilarvirus; D012313:RNA; D001120:Arginine; D004722:Endoribonucleases; C022543:ribonuclease T(2)