Novel catalytic activity associated with positive-strand RNA virus infection: nucleic acid-stimulated ATPase activity of the plum pox potyvirus helicaselike protein.
The cylindrical inclusion protein of potyviruses contains the so-called nucleoside triphosphate binding motif, an amino acid sequence motif present in proteins encoded by most positive-strand RNA viruses, some double-strand RNA viruses, apparently all groups of double-strand DNA viruses, and also several single-strand DNA viruses. Further sequence analysis has allowed to include the cylindrical inclusion protein of potyviruses as a member of a superfamily of helicaselike proteins. In this paper we show that the purified cylindrical inclusion protein of plum pox potyvirus interacts with RNA and ATP and copurifies with a nucleic acid-stimulated ATPase activity. To our knowledge, this is the first time that this kind of enzymatic activity has been experimentally associated with a positive-strand RNA virus-encoded protein.
Laín
S
S
Centro de Biología Molecular (Consejo Superior de Investigaciones Cientificas-Universidad Autónoma de Madrid, Spain.
Martín
M T
MT
Riechmann
J L
JL
García
J A
JA
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D004265:DNA Helicases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D010942:Plant Viruses / Q000201:enzymology*; D011061:Poly A / Q000302:isolation & purification / Q000378:metabolism*; D012328:RNA Viruses / Q000201:enzymology*; D014466:Ultraviolet Rays
D011061:Poly A; D000251:Adenosine Triphosphatases; D004265:DNA Helicases