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Title: Characterization of the nuclear localization signal of high risk HPV16 E2 protein

The E2 protein of high risk human papillomavirus type 16 (HPV16) contains an amino-terminal (N) domain, a hinge (H) region and a carboxyl-terminal (C) DNA-binding domain. Using enhanced green fluorescent protein (EGFP) fusions with full length E2 and E2 domains in transfection assays in HeLa cells, we found that the C domain is responsible for the nuclear localization of E2 in vivo, whereas the N and H domains do not contain additional nuclear localization signals (NLSs). Deletion analysis of EGFP-E2 and EGFP-cE2 determined that the C domain contains an {alpha} helix cNLS that overlaps with the DNA-binding region. Mutational analysis revealed that the arginine and lysine residues in this cNLS are essential for nuclear localization of HPV16 E2. Interestingly, these basic amino acid residues are well conserved among the E2 proteins of BPV-1 and some high risk HPV types but not in the low risk HPV types, suggesting that there are differences between the NLSs and corresponding nuclear import pathways between these E2 proteins.
Authors:
 [1] ;  [1] ;  [1] ;  [1] ;  [2]
  1. Biology Department, Boston College, Higgins Hall, room 578, 140 Commonwealth Avenue, Chestnut Hill, MA 02467 (United States)
  2. Biology Department, Boston College, Higgins Hall, room 578, 140 Commonwealth Avenue, Chestnut Hill, MA 02467 (United States). E-mail: moroianu@bc.edu
Publication Date:
OSTI Identifier:
20977005
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 360; Journal Issue: 1; Other Information: DOI: 10.1016/j.virol.2006.10.018; PII: S0042-6822(06)00749-5; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ARGININE; DNA; HEALTH HAZARDS; HELA CELLS; IN VIVO; LYSINE; PROTEINS; SIGNALS