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Structure and expression of the equine infectious anemia virus transcriptional trans-activator (tat).

Abstract: Equine infectious anemia virus (EIAV) encodes a tat gene which is closely related to the trans-activators encoded by the human and simian immunodeficiency viruses. Nucleotide sequence analysis of EIAV cDNA clones revealed that the tat message is composed of three exons; the first two encode tat and the third may encode rev.. Interestingly, EIAV tat translation is initiated at a non-AUG codon in the first exon of the message, perhaps allowing an additional level of gene regulation. The deduced amino acid sequence of EIAV tat, combined with functional analyses of tat cDNAs in transfected cells, have provided some unique insights into the domain structure of this protein. EIAV Tat has a C-terminal basic domain, a highly conserved 16 amino acid core domain, but not the cysteine-rich region, that is present in the primate immunodeficiency virus Tat proteins. Thus EIAV encodes a relatively simple version of this kind of trans-activator.
Publication Date: 1990-01-01 PubMed ID: 2178129
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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The research article discusses the structure and expression of the Tat gene in Equine Infectious Anemia Virus (EIAV). It reveals that the gene is divided into three exons, with the first two encoding for Tat and the third possibly for Rev. The study also explores unique functionality of Tat cDNAs in transfected cells.

Nature of Research and Methodology

  • The research focuses on understanding the composition of the Equine infectious anemia virus (EIAV) through the analysis of its tat gene.
  • Using nucleotide sequence analysis of EIAV cDNA clones as their main methodology, the researchers discovered the three-exon structure of the tat message.
  • The first two exons were found to encode tat, while the third exon was suggested to possibly encode another gene, rev.
  • The researchers also found that EIAV tat translation begins at a non-AUG codon in the first exon, hinting at another level of gene regulation.

Findings and Insights

  • The research indicates that EIAV Tat has a C-terminal basic domain, a highly conserved 16 amino acid core domain, but it lacks the cysteine-rich region that’s present in the primate immunodeficiency virus Tat proteins.
  • This differentiation suggests that EIAV encodes a simpler version of the trans-activator protein, compared to prime immunodeficiency viruses.
  • By combining the deduced amino acid sequence of EIAV tat with functional analysis of tat cDNAs in transfected cells, the researchers gained unique insights into the domain structure of this protein.

Implication and Significance

  • Understanding the unique properties of EIAV could be instrumental in the development of new therapeutic approaches and vaccines to combat Equine Infectious Anemia.
  • Further study of the EIAV Tat protein could also help researchers understand more about viral gene regulation, given the identified presence of a non-AUG codon initiation in this protein.

Cite This Article

APA
Derse D, Dorn P, DaSilva L, Martarano L. (1990). Structure and expression of the equine infectious anemia virus transcriptional trans-activator (tat). Dev Biol Stand, 72, 39-48.

Publication

ISSN: 0301-5149
NlmUniqueID: 0427140
Country: Switzerland
Language: English
Volume: 72
Pages: 39-48

Researcher Affiliations

Derse, D
  • Laboratory of Viral Carcinogenesis, National Cancer Institute, Frederick, MD 21701.
Dorn, P
    DaSilva, L
      Martarano, L

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Base Sequence
        • Blotting, Northern
        • Cell Line
        • Cloning, Molecular
        • DNA, Viral / genetics
        • Exons
        • Gene Expression Regulation, Viral
        • Gene Products, tat / chemistry
        • Gene Products, tat / genetics
        • Genes, tat
        • Infectious Anemia Virus, Equine / genetics
        • Molecular Sequence Data
        • Open Reading Frames
        • Protein Biosynthesis
        • RNA, Viral / genetics
        • Restriction Mapping
        • Transcription, Genetic
        • Transcriptional Activation
        • Transfection

        Grant Funding

        • N01-CO-74102 / NCI NIH HHS

        Citations

        This article has been cited 2 times.
        1. Taube R, Fujinaga K, Irwin D, Wimmer J, Geyer M, Peterlin BM. Interactions between equine cyclin T1, Tat, and TAR are disrupted by a leucine-to-valine substitution found in human cyclin T1.. J Virol 2000 Jan;74(2):892-8.
          doi: 10.1128/jvi.74.2.892-898.2000pubmed: 10623752google scholar: lookup
        2. Harris ME, Gontarek RR, Derse D, Hope TJ. Differential requirements for alternative splicing and nuclear export functions of equine infectious anemia virus Rev protein.. Mol Cell Biol 1998 Jul;18(7):3889-99.
          doi: 10.1128/MCB.18.7.3889pubmed: 9632773google scholar: lookup