Association of Tat protein and viral mRNA with nuclear matrix from HIV-1-infected H9 cells

• Published in: Biochimica et biophysica acta, Protein structure and molecular enzymology Vol. 1008; no. 2; pp. 208 - 212
• Main Authors: Mueller, WEG, Wenger, R, Reuter, P, Renneisen, K, Schroeder, H C
• Format: Journal Article
• Language: English
• Published: 01.01.1989
• Subjects: human immunodeficiency virus 1
• ISSN: 0167-4838

The transactivating protein from human immunodeficiency virus type 1 (HIV-1), Tat, was found to bind to the nuclear matrix from uninfected and HIV-1-infected H9 cells. Addition of the Zn super(2+), Cd super(2+) and Cu super(2+) chelator o-phenanthroline destroyed the matrix fibrils and the binding affinity of Tat to the matrix. A sequential treatment of the matrix, first with o-phenanthroline and then with ZnCl sub(2), partially restored the fibrillar-like matrix structure. Infection of H9 cells with HIV-1 resulted in a displacement of cellular mRNA by viral mRNA from the nuclear matrix. Both the matrix-bound host cell and HIV-1 mRNA were found to dissociate from the matrix in the presence of o-phenanthroline. This could be prevented by coincubation with Zn super(2+) or Cu super(2+) (but not Mg super(2+)), which stabilize the mRNA containing nuclear matrix structure.