Adenovirus type 2 endopeptidase: An unusual phosphoprotein enzyme matured by autocatalysis

P. K. Chatterjee, S. J. Flint

Research output: Contribution to journalArticle

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Abstract

A 19-kDa protein, present in low copy number in purified adenovirus type 2, has been characterized. Several criteria were used to establish that this protein is neither a degradation product of the known structural proteins of the virion nor a minor, unusually modified, form of protein VII. This 19-kDa protein, unlike other virion proteins, possesses alkali-resistant phosphoamino acids. Analysis by partial proteolysis indicated that it is related to a 23-kDa phosphoprotein present in H2ts-1 virions assembled in infected cells maintained at 39°C. Affinity labeling with [3H]diisopropyl fluorophosphate showed that the 19-kDa protein contains the active site for a serine protease. We, therefore, conclude that the 19-kDa protein is the active form of the adenovirus-encoded endopeptidase, defined by the H2ts-1 mutation, and is synthesized as a 23-kDa precursor that appears to mature by autocatalysis.

Original languageEnglish (US)
Pages (from-to)714-718
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number3
DOIs
StatePublished - 1987

All Science Journal Classification (ASJC) codes

  • General

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