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Human T-cell leukemia virus type 1 reverse transcriptase (RT) originates from the pro and pol open reading frames and requires the presence of RT-RNase H (RH) and RT-RH-integrase proteins for its activity.
- Source :
-
Journal of virology [J Virol] 1998 Aug; Vol. 72 (8), pp. 6504-10. - Publication Year :
- 1998
-
Abstract
- The first description of an active form of a recombinant human T-cell leukemia virus type 1 (HTLV-1) reverse transcriptase (RT) and subsequent predictions of its amino acid sequence and quaternary structure are reported here. By using amino acid alignment methods, the NH2 and COOH termini of the RT, RNase H (RH), and integrase (IN) domains of the Pol polyprotein were determined. The HTLV-1 RT seems to be unique since its NH2 terminus is probably encoded by the pro open reading frame (ORF) fused downstream, via a transframe peptide, to the polypeptide encoded by the pol ORF. The HTLV-1 Pol amino acid sequence was revealed to be highly similar to that of Rous sarcoma virus (RSV), particularly at the RT-RH hinge region. These two domains remain linked for RSV; this may also be the case for HTLV-1. In light of these results, RT, RT-RH, and RT-RH-IN genes were constructed and introduced into His-tagged protein expression vectors. The corresponding proteins were synthesized in vitro, and the DNA polymerase activities of different protein combinations were tested. Solely the RT-RH-RT-RH-IN combination was found to have a significant activity level. Velocity sedimentation analysis suggested that the HTLV-1 RT-RH and RT-RH-IN monomers are likely associated in an oligomeric structure, probably of the alpha3/beta type.
- Subjects :
- Amino Acid Sequence
Binding Sites
Genetic Vectors
Human T-lymphotropic virus 1 genetics
Humans
Molecular Sequence Data
Peptides
Protein Conformation
Protein Precursors genetics
Protein Precursors metabolism
Proteins genetics
Proteins metabolism
RNA-Directed DNA Polymerase chemistry
Genes, pol
Histidine
Human T-lymphotropic virus 1 enzymology
Integrases metabolism
Open Reading Frames
RNA-Directed DNA Polymerase metabolism
Ribonuclease H metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0022-538X
- Volume :
- 72
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Journal of virology
- Publication Type :
- Academic Journal
- Accession number :
- 9658093
- Full Text :
- https://doi.org/10.1128/JVI.72.8.6504-6510.1998