Coat proteins of two filamentous plant viruses display NTPase activity in vitro.
Coat proteins (CPs) of plant viruses are involved in different stages of the viral life cycle such as virion assembly, replication, movement, vector transmission, and regulation of host defense responses. Here, we report that the CPs of two filamentous RNA viruses, potato virus X (PVX, Potexvirus) and potato virus A (PVA, Potyvirus) exhibit an enzyme activity. The CP isolated from PVX virions possesses ATP-binding and ATPase activities. Recombinant PVX and PVA CPs produced in Escherichia coli show Mg2+-dependent ATPase and UTPase activities inhibited by antibodies against virus particles. Deletion of the C-terminal regions of these proteins diminishes their ATPase activity.
Rakitina
Daria V
DV
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia. rakitina@genebee.msu.su
Kantidze
Omar L
OL
Leshchiner
Anna D
AD
Solovyev
Andrey G
AG
Novikov
Viktor K
VK
Morozov
Sergey Yu
SY
Kalinina
Natalia O
NO
D000255:Adenosine Triphosphate / Q000378:metabolism; D036022:Capsid Proteins / Q000235:genetics / Q000378:metabolism*; D008274:Magnesium / Q000378:metabolism; D043583:Nucleoside-Triphosphatase / Q000235:genetics / Q000378:metabolism*; D017863:Potexvirus / Q000201:enzymology*; D017800:Potyvirus / Q000201:enzymology*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014771:Virion / Q000378:metabolism
D036022:Capsid Proteins; D011994:Recombinant Proteins; D000255:Adenosine Triphosphate; D043583:Nucleoside-Triphosphatase; D008274:Magnesium