Abstract
The tat protein of human immunodeficiency virus (HIV) has a characteristic cysteine-rich region containing 7 cysteines within 16 residues. The role of this region was investigated by creation of several tat gene mutants. The activities of the novel tat gene translational products were assayed by measuring the cotransfected chloramphenicol acetyl-transferase (CAT) gene expression controlled by HIV long-terminal repeat (LTR) in the COS 7 cells. Substitution of either Cys22 with Gly, or Cys34-Gln-Val-Cys with His-Gln-Val-His, and deletion behind Lys50 of the tat protein caused a drastic loss in its activity.
Original language | English |
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Pages (from-to) | 113-118 |
Number of pages | 6 |
Journal | Virus Genes |
Volume | 2 |
Issue number | 2 |
DOIs | |
Publication status | Published - Mar 1 1989 |
Externally published | Yes |
Keywords
- CAT assay
- HIV tat protein
- cysteine-rich region
- site-directed mutagenesis
- trans-activation
- zinc-finger motif
ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Virology