Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization

6533b7dafe1ef96bd126ed54

RESEARCH PRODUCT

Dissection of human papillomavirus type 33 L2 domains involved in nuclear domains (ND) 10 homing and reorganization

Luise Florin Cornelia Sapp Martin Sapp Katrin A. Becker

subject

Immunoprecipitation Recombinant Fusion Proteins Green Fluorescent Proteins Nuclear Localization Signals Active Transport Cell Nucleus Fluorescent Antibody Technique Biology Immunofluorescence Autoantigens Green fluorescent protein Death-associated protein 6 Daxx Virology Tumor Cells Cultured medicine Sp100 Humans NLS Papillomaviridae Adaptor Proteins Signal Transducing Cell Nucleus medicine.diagnostic_test Intracellular Signaling Peptides and Proteins ND10 Nuclear Proteins Antigens Nuclear L2 Oncogene Proteins Viral Papillomavirus biochemical phenomena metabolism and nutrition Molecular biology Deletion Mutagenesis Luminescent Proteins Capsid Mutagenesis Capsid Proteins Carrier Proteins Co-Repressor Proteins Gene Deletion Nuclear localization sequence Molecular Chaperones

description

Abstract We have recently shown that the minor capsid protein L2 of human papillomavirus type 33 (HPV33) recruits the transcriptional repressor Daxx into nuclear domains (ND) 10 and causes the loss of the transcriptional activator Sp100 from these subnuclear structures (Florin et al., 2002b) . In order to dissect L2 domains involved in nuclear translocation, ND10 homing, loss of Sp100, and recruitment of Daxx, a detailed deletion mutagenesis of L2 was performed. Using immunofluorescence and green fluorescent protein fusions, we have identified two nuclear localization signals (NLS) in the central and C-terminal part of L2, respectively, homologous to previously identified NLS in HPV6B L2 (Sun et al., 1995) . We mapped the ND10 localization domain to within a 30 amino acid peptide in the C-terminal half of L2. L2-induced attraction of Daxx into ND10, coimmunoprecipitation of L2 and Daxx, as well as induction of the loss of Sp100 from ND10 require an intact ND10 localization domain. This domain contains conserved PXXP motives characteristic of some protein/protein interacting domains. Our data also suggest that the Daxx/L2 interaction may be the driving force for L2 accumulation in ND10.

year	journal	country	edition	language
2003-09-01	Virology

https://doi.org/10.1016/s0042-6822(03)00447-1