Document 0424 DOCN M9590424 TI Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins. DT 9509 AU Fridell RA; Harding LS; Bogerd HP; Cullen BR; Howard Hughes Medical Institute, Durham, North Carolina, USA. SO Virology. 1995 Jun 1;209(2):347-57. Unique Identifier : AIDSLINE GENBANK/U18543 AB 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. DE Amino Acid Sequence Animal Binding Sites Cell Line Cell Nucleus/*METABOLISM Cercopithecus aethiops Chloramphenicol Acetyltransferase/ANALYSIS/BIOSYNTHESIS Comparative Study DNA, Complementary Gene Products, tat/*METABOLISM Hela Cells Human HIV-1/GENETICS/*METABOLISM HIV-2/*METABOLISM Kidney Molecular Sequence Data Recombinant Proteins/ANALYSIS/BIOSYNTHESIS Sequence Homology, Amino Acid Transcription Factors/*METABOLISM Transfection Zinc Fingers/*PHYSIOLOGY JOURNAL ARTICLE SOURCE: National Library of Medicine. NOTICE: This material may be protected by Copyright Law (Title 17, U.S.Code).