ATP hydrolysis and AMP kinase activities of nonstructural protein 2C of human parechovirus 1.
The highly conserved picornavirus 2C proteins, thought to be involved in genome replication, contain three motifs found in NTPases/helicases of superfamily III. We report that human parechovirus 1 2C displays Mg2+-dependent ATP diphosphohydrolase activity in vitro, whereas other nucleoside triphosphates are not substrates for the hydrolysis. We also found that the 2C protein has an enzymatic activity that converts AMP to a corresponding diphosphate using ADP or ATP as a phosphate donor. In addition, we observed that ATP hydrolysis results in 2C autophosphorylation. These findings indicate that the parechovirus 2C protein has enzymatic activities, which may contribute to several functions in the viral replication cycle.
Samuilova
Olga
O
Haartman Institute, Department of Virology, P.O. Box 21, FIN-00014 University of Helsinki, Helsinki, Finland. olga.samuildva@helsinki.fi
Krogerus
Camilla
C
Fabrichniy
Igor
I
Hyypiä
Timo
T
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000263:Adenylate Kinase / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D006868:Hydrolysis; D008274:Magnesium; D030061:Parechovirus / Q000201:enzymology / Q000502:physiology*; D010766:Phosphorylation; D010850:Picornaviridae Infections; D017361:Viral Nonstructural Proteins / Q000378:metabolism*; D014779:Virus Replication
D002352:Carrier Proteins; D017361:Viral Nonstructural Proteins; D000255:Adenosine Triphosphate; D000263:Adenylate Kinase; C076023:2C protein, viral; D008274:Magnesium