Autoprocessing of HSV-1 protease: effect of deletions on autoproteolysis.
HSV-1 protease is involved in virus maturation. It is autoproteolytic and processed from a larger precursor. We have analysed the autoproteolysis of UL26 ORF and shown by in vitro-coupled transcription and translation that the UL26 encoded protein is processed, leading to the accumulation of its N-terminal domain. The deletion of the residues 245-248 in UL26 ORF abolishes the N-terminal cleavage but not the C-terminal processing. Deletion of the 3' end of UL26 prevents production of the mature protease. These results strongly suggest that autoproteolysis is achieved in a defined order.
Godefroy
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S
Marion Merrell Dow Research Institute, Strasbourg, France.
Guenet
C
C
D000595:Amino Acid Sequence; D001483:Base Sequence; D017931:DNA Primers; D018259:Herpesvirus 1, Human / Q000235:genetics / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D011499:Protein Processing, Post-Translational; D017384:Sequence Deletion; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
D017931:DNA Primers; D014764:Viral Proteins; C079287:scaffold protein, Herpes simplex virus-1; D012697:Serine Endopeptidases