Autoprocessing of HSV-1 protease: effect of deletions on autoproteolysis

• Published in: FEBS letters Vol. 357; no. 2; pp. 168 - 172
• Main Authors: Godefroy, Sylvie, Guenet, Chantal
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 03.01.1995
• Subjects: Amino Acid Sequence; Autoproteolysis; Base Sequence; CMV; cytomegalovirus; DNA Primers; herpes simplex virus 1; Herpes simplex virus type 1; Herpesvirus 1, Human - genetics; Herpesvirus 1, Human - metabolism; HSV-1; HSV-1 protease; Hydrolysis; ICP35; In vitro transcription translation; infected cell proteins 35; Molecular Sequence Data; open reading frame; Open Reading Frames; ORF; Protein Processing, Post-Translational; Sequence Deletion; Serine Endopeptidases - genetics; Serine Endopeptidases - metabolism; UL26 open reading frame; Viral Proteins - genetics; Viral Proteins - metabolism; In vitro transcription translation; HSV-1; ORF; HSV-1 protease; Autoproteolysis; UL26 open reading frame; ICP35; CMV
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(94)01352-2

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.