Specific binding of the human T-cell leukemia virus type I Rex protein to a short RNA sequence located within the Rex-response element.
Expression of the structural proteins of human T-cell leukemia virus type I is dependent upon the interaction of the viral Rex trans activator with its highly structured cis-acting RNA target sequence, the 254-nucleotide Rex-response element. Nucleotides critical for Rex binding in vitro have been mapped by modification interference analysis to a discrete 12-nucleotide RNA sequence that is predicted to form a stem-bulge-stem structure. This minimal RNA binding site was sufficient to mediate specific Rex binding in vitro when analyzed in the context of a short RNA probe. The critical importance of this short RNA sequence in mediating Rex function in vivo is supported by its complete conservation among all primate T-cell leukemia virus isolates.
Bogerd
H P
HP
Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710.
Tiley
L S
LS
Cullen
B R
BR
D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D016370:Gene Products, rex / Q000378:metabolism*; D015368:Human T-lymphotropic virus 1 / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D016133:Polymerase Chain Reaction; D015347:RNA Probes; D012326:RNA Splicing; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D015534:Trans-Activators / Q000378:metabolism
D016370:Gene Products, rex; D015347:RNA Probes; D012367:RNA, Viral; D015534:Trans-Activators