HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Takramah, D. Articles by Häcker, G. Search for Related Content PubMed PubMed Citation Articles by Takramah, D. Articles by Häcker, G. Agricola Articles by Takramah, D. Articles by Häcker, G.

Baculovirus P35 interacts with a subunit of human RNA polymerase II and can enhance promoter activity in human cells

Sophie Schaller^2,

Marc Vigneron^2,

¹ Institute for Medical Microbiology, Immunology and Hygiene, Technische Universität München, Trogerstr. 9, D-81675 Munich, Germany
² Institut de Genetique et de Biologie Moleculaire et Cellulaire (CNRS/INSERM/ULP), Illkirch, France

Correspondence
Georg Häcker
hacker{at}lrz.tum.de

The early protein P35 from the baculovirus Autographa californica nucleopolyhedrovirus is a direct inhibitor of caspases and can block apoptosis in a wide variety of systems. In addition, it has been linked to the regulation of viral gene expression, shut-down of protein synthesis in infected insect cells and malignant transformation of mouse fibroblasts. By yeast-two-hybrid screening we identified the RPB11a subunit of human RNA polymerase II as an interaction partner of P35. Specificity of the interaction was confirmed by affinity blotting. By immunocytology, P35 was in part found in the nucleus of transfected cells. Homology searches further revealed that P35 has structural similarity with RPB3, the subunit of RNA polymerase II that has been demonstrated to interact directly with RPB11a. When transfected into human colon carcinoma cells, P35 was able to enhance the activity of E-cadherin and -actin promoters by about a factor of two as measured by luciferase reporter assay. P35 and hRPB11a together enhanced the E-cadherin activity about three- to fourfold. These data suggest an additional role for P35 in the regulation of cellular transcription.

Published ahead of print on 22 August 2003 as DOI 10.1099/vir.0.19395-0.

Present address: Nordic Bioscience A/S, Herlev Hovedgade 207, 2730 Herlev, Denmark.

Present address: UMR 7100, CNRS-ULP, ESBS, Boulevard Sebastien Brant, BP 10413, 67412 Illkirch Cedex, France.