Characterization of a protein kinase gene from two Chlorella viruses.
An open reading frame (ORF) with strong homology to eukaryotic serine/threonine protein kinases was found in the two Chlorella viruses SC-1A and PBCV-1. The deduced molecular weights of each putative protein kinase were 35 kDa and the predicted amino acid sequences of the two proteins were 95% identical. The ORF encoding the SC-1A protein kinase was over-expressed as a fusion protein in Escherichia coli. The recombinant fusion protein had autophosphorylation activity and could phosphorylate certain exogenous proteins. Antiserum against the recombinant fusion protein reacted with a 35 kDa protein plus three larger proteins from virus infected cells. The 35 kDa protein was a late protein; however, the 35 kDa protein was not packaged in the virion, even though virions contain protein kinase activity.
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Department of Plant Pathology, University of Nebraska, Lincoln 68583-0722, USA.
Van Etten
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JL
D000595:Amino Acid Sequence; D001483:Base Sequence; D002708:Chlorella / Q000821:virology*; D017124:Conserved Sequence; D017931:DNA Primers; D004926:Escherichia coli; D015967:Gene Expression Regulation, Viral; D008969:Molecular Sequence Data; D010766:Phosphorylation; D017862:Phycodnaviridae / Q000201:enzymology*; D017346:Protein Serine-Threonine Kinases / Q000235:genetics* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D014158:Transcription, Genetic
D017931:DNA Primers; D011993:Recombinant Fusion Proteins; D017346:Protein Serine-Threonine Kinases