Dual role of the adenovirus pVI C terminus as a nuclear localization signal and activator of the viral protease.

KS Honkavuori, BD Pollard, MS Rodriguez, RT Hay, Graham Duncan Kemp

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

Adenain, the protease produced by adenovirus, is regulated by formation of a heterodimer with an 11 aa peptide derived from the C terminus of another adenoviral protein, pVI. Here, the role of the basic motif KRRR, which is conserved in pVI sequences from human adenovirus serotypes, was investigated. It was shown that this motif is less important than the N- or C-terminal regions in the formation of the adenain-pepticle heterodimer and in the activity of the subsequent complex. This motif, however, acted as a nuclear localization signal that was capable of targeting heterologous proteins to the nucleus, resulting in a distinctive intranuclear distribution consisting of discrete foci, which is similar to that found for pVI during adenovirus infection.

Original languageEnglish
Pages (from-to)3367 - 3376
Number of pages10
JournalJournal of General Virology
Volume85
Issue number11
DOIs
Publication statusPublished - Nov 2004

Keywords

  • PROTEINASE ACTIVITY
  • PEPTIDE
  • TYPE-2
  • POLYPEPTIDE
  • COFACTOR
  • CLEAVAGE
  • LOCATION
  • CELLS

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