Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein

Cell. 1988 Dec 23;55(6):1179-88. doi: 10.1016/0092-8674(88)90262-0.


HIV-1 encodes a potent trans-activator protein, tat, which is essential for viral gene expression. To study tat domains that function in trans-activation, we chemically synthesized the 86 amino acid tat protein (tat-86) and tat mutant peptides. Remarkably, tat-86 is rapidly taken up by cells, and produces a massive and specific stimulation of HIV-LTR-driven RNA synthesis. Mutant peptides of 21 to 41 amino acids exhibit significant activity. Only two regions are essential for trans-activation; we suggest that one represents an activation region and the other, a nucleic acid binding or nuclear targeting region. Amino acid substitutions within these regions greatly reduce trans-activation, demonstrating the functional significance of these domains. The N-terminal 37 amino acids and exon 2 are not essential. Thus, tat is similar to regulatory proteins of Ad E1A and BPV1 E5 oncogenes, requiring only small domains for autonomous function.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Chromosome Deletion
  • Gene Expression Regulation*
  • Gene Products, tat
  • Genes, Viral*
  • HIV-1 / genetics*
  • Microinjections
  • Mutation
  • Oncogenes
  • RNA, Viral / biosynthesis
  • Transcription Factors / analysis
  • Transcription Factors / chemical synthesis*
  • Transcription Factors / pharmacology
  • tat Gene Products, Human Immunodeficiency Virus


  • Gene Products, tat
  • RNA, Viral
  • Transcription Factors
  • tat Gene Products, Human Immunodeficiency Virus