Echovirus 9 strain Barty non-structural protein 2C has NTPase activity

Non-structural protein 2C is known to play a fundamental role in the replication of picornaviruses. Sequence analyses revealed that 2C belongs to a rapidly expanding group of proteins containing a consensus sequence for nucleotide binding (NTB). We report that echovirus 9 polypeptide 2C displays NTP...

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Bibliographic Details
Published in:Virus research 1999-12, Vol.65 (2), p.155-160
Main Authors: Klein, Marcus, Eggers, Hans J, Nelsen-Salz, Birgit
Format: Article
Language:English
Subjects:
Acid Anhydride Hydrolases - metabolism
Adenosine Triphosphatases - metabolism
ATPase
DNA-Binding Proteins - biosynthesis
DNA-Binding Proteins - metabolism
Echovirus 9
Echovirus 9 - enzymology
Enterovirus
Escherichia coli - genetics
Escherichia coli - metabolism
Genetic Vectors - genetics
GTP Phosphohydrolases - metabolism
GTPase
Human echovirus 9
NTPase
Nucleoside-Triphosphatase
Nucleotide binding (NTB) motif
Pircornaviridae
Protein 2C
RNA Helicases - biosynthesis
RNA Helicases - metabolism
Transfection - genetics
Viral Proteins
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Summary:Non-structural protein 2C is known to play a fundamental role in the replication of picornaviruses. Sequence analyses revealed that 2C belongs to a rapidly expanding group of proteins containing a consensus sequence for nucleotide binding (NTB). We report that echovirus 9 polypeptide 2C displays NTPase activity in vitro. In our experiments, several P2 genes were expressed in Escherichia coli as fusion proteins linked to glutathione S-transferase (GST) prior to purification close to homogeneity. In contrast to GST-2B, both GST-2C and GST-2BC showed ATPase as well as GTPase activity indicating that the site for NTB binding and splitting is located in 2C.
ISSN:0168-1702
1872-7492
DOI:10.1016/S0168-1702(99)00110-0