Abstract
In vitro-synthesized human T-cell leukemia virus type 1 (HTLV-I) Rex response element (Rex-RE) activates the interferon-induced 2′, 5′-oligoadenylate synthetase (2-5OAS) in a dose-dependent manner. In addition, Rex-RE at 1 μg/ml activates a second interferon-induced enzyme, p68 kinase (PKR); however, at 50 μg/ml, Rex-RE inhibits PKR activity. Poly(rl)-poly(rC) (10 μg/ml) dissociates the ribonucleoprotein complexes, Rex-RE/2-5OAS, or Rex-RE/PKR, whereas poly(rC) (100 μ/ml) does not, indicating the presence of high affinity interactions between Rex-RE and these two enzymes. To further characterize the interaction of Rex-RE with 2-5OAS and PKR, [ 32P]Rex-RE was uv-cross-linked to 2-5OAS and PKR present in interferontreated HeLa cell extracts. The affinity of Rex-RE to highly purified 4O-kDa human recombinant 2-5OAS was determined to be K d = 4.7 n M. The relevance of these results to the pathogenesis of HTLV-I associated adult T-cell leukemia/lymphoma is discussed.
Published Version
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