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Autoprocessing of HSV‐1 protease: effect of deletions on autoproteolysis
Author(s) -
Godefroy Sylvie,
Guenet Chantal
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01352-2
Subject(s) - protease , cleavage (geology) , transcription (linguistics) , messenger rna , biology , chemistry , microbiology and biotechnology , biochemistry , enzyme , gene , paleontology , linguistics , philosophy , fracture (geology)
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.