Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins. 1995

R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
Howard Hughes Medical Institute, Durham, North Carolina, USA.

Transcriptional activation of HIV-1 gene expression by the viral Tat protein requires the interaction of a cellular cofactor with the Tat activation domain. This domain has been shown to consist of the cysteine-rich and core motifs of HIV-1 Tat and is functionally conserved in the distantly related Tat proteins of HIV-2 and EIAV. Using the yeast two-hybrid system, we have identified a novel human gene product, termed HT2A, that specifically and precisely binds to the activation domain of HIV-1 Tat and that can also interact with the HIV-2 and EIAV Tat proteins in vivo. We present data further demonstrating that the interaction between the activation domain of HIV-1 Tat and the HT2A protein can be readily detected in the mammalian cell nucleus. Sequence analysis demonstrates that HT2A is a novel member of the C3HC4 or ring finger family of zinc finger proteins that includes several known oncogenes and transcription factors. Overall, these data suggest that HT2A may play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo.

UI MeSH Term Description Entries
D007668 Kidney Body organ that filters blood for the secretion of URINE and that regulates ion concentrations. Kidneys
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D002467 Cell Nucleus Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed) Cell Nuclei,Nuclei, Cell,Nucleus, Cell
D002522 Chlorocebus aethiops A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research. African Green Monkey,Cercopithecus aethiops,Cercopithecus griseoviridis,Cercopithecus griseus,Cercopithecus pygerythrus,Cercopithecus sabeus,Cercopithecus tantalus,Chlorocebus cynosuros,Chlorocebus cynosurus,Chlorocebus pygerythrus,Green Monkey,Grivet Monkey,Lasiopyga weidholzi,Malbrouck,Malbrouck Monkey,Monkey, African Green,Monkey, Green,Monkey, Grivet,Monkey, Vervet,Savanah Monkey,Vervet Monkey,Savannah Monkey,African Green Monkey,Chlorocebus cynosuro,Green Monkey, African,Green Monkeys,Grivet Monkeys,Malbrouck Monkeys,Malbroucks,Monkey, Malbrouck,Monkey, Savanah,Monkey, Savannah,Savannah Monkeys,Vervet Monkeys
D006367 HeLa Cells The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for, among other things, VIRUS CULTIVATION and PRECLINICAL DRUG EVALUATION assays. Cell, HeLa,Cells, HeLa,HeLa Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000070584 Tripartite Motif Proteins A protein family defined by the presence of three ZINC FINGER domains, one of which is a RING FINGER DOMAIN, a coiled-coil region, and a highly variable C-terminal region. They function in many cellular processes including APOPTOSIS and CELL CYCLE regulation. RBCC Protein,TRIM Protein,Tripartite Motif Protein,RBCC Protein Family,RBCC Proteins,TRIM Protein Family,TRIM Proteins,Family, RBCC Protein,Family, TRIM Protein,Motif Protein, Tripartite,Motif Proteins, Tripartite,Protein Family, RBCC,Protein Family, TRIM,Protein, RBCC,Protein, TRIM,Protein, Tripartite Motif,Proteins, RBCC,Proteins, TRIM,Proteins, Tripartite Motif
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

Related Publications

R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
June 2001, The Journal of biological chemistry,
R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
September 2005, Genes to cells : devoted to molecular & cellular mechanisms,
R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
April 1997, The Journal of biological chemistry,
R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
October 2003, FEBS letters,
R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
March 2003, Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica,
R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
December 1994, The Journal of biological chemistry,
R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
August 2000, Biochemical and biophysical research communications,
R A Fridell, and L S Harding, and H P Bogerd, and B R Cullen
June 2007, FEBS letters,
Copied contents to your clipboard!