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1: Biochim Biophys Acta. 1989 Jul 7;1008(2):208-12.Click here to read Links

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

Müller WE, Wenger R, Reuter P, Renneisen K, Schröder HC.

Abteilung Angewandte Molekularbiologie, Universität, Mainz, F.R.G.

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 Zn2+, Cd2+ and Cu2+ 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 ZnCl2, 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 Zn2+ or Cu2+ (but not Mg2+), which stabilize the mRNA containing nuclear matrix structure.

PMID: 2544227 [PubMed - indexed for MEDLINE]