ATP binding and ATPase activities associated with recombinant rabbit hemorrhagic disease virus 2C-like polypeptide.
The carboxy-terminal region of the rabbit hemorrhagic disease virus p37 polyprotein cleavage product has been expressed in Escherichia coli as a glutathione S-transferase (GST) fusion protein. The recombinant GST-Delta2C protein showed in vitro ATP-binding and ATPase activities. Site-directed mutagenesis studies of the conserved residues G(522) and T(529) in motif A, D(566) and E(567) in motif B, and K(600) in motif C were also performed. These results provide the first experimental characterization of a 2C-like ATPase activity in a member of the Caliciviridae.
Marín
M S
MS
Departamento de Bioquímica y Biología Molecular, Instituto Universitario de Biotecnología de Asturias (CSIC), Universidad de Oviedo, 33006 Oviedo, Spain.
Casais
R
R
Alonso
J M
JM
Parra
F
F
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism*; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D017929:Hemorrhagic Disease Virus, Rabbit / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D017361:Viral Nonstructural Proteins / Q000235:genetics* / Q000378:metabolism*
D002352:Carrier Proteins; D011993:Recombinant Fusion Proteins; D017361:Viral Nonstructural Proteins; D000255:Adenosine Triphosphate; D005982:Glutathione Transferase; C076023:2C protein, viral; D000251:Adenosine Triphosphatases