TY - JOUR
T1 - The hepatitis B virus posttranscriptional regulatory element is composed of two subelements
AU - Donello, John E.
AU - Beeche, Arlyne A.
AU - Smith, George J.
AU - Lucero, Ginger R.
AU - Hope, Thomas J.
PY - 1996
Y1 - 1996
N2 - The RNAs of the hepatitis B virus (HBV) contain a cis-acting regulatory element which facilitates the cytoplasmic localization of unspliced transcripts (J. Huang and T. J. Liang, Mol. Cell. Biol. 13:7476-7486, 1993, and Z. M. Huang and T. S. Yen, J. Virol. 68:3193-3199, 1994). Such localization is presumed to be mediated by cellular factors which interact with the element. The HBV posttranscriptional regulatory element (HBVPRE) can efficiently activate an RNA export reporter system in an orientation-dependent and position-independent manner. Deletion analysis reveals that the HBVPRE consists of two subelements which function synergistically. A synergistic effect was also observed when the 5′ (PREα) or 3′ (PREβ) subelements were duplicated. The bipartite structure of the HBVPRE is reminiscent of reports that the high-affinity binding sites of the Rev-like proteins must be duplicated to function efficiently (M. Grone, E. Hoffmann, S. Berchtold, B. R. Cullen, and R. Grassmann, Virology 204:144-152,1994; X. Huang, T. J. Hope, B. L. Bond, D. McDonald, K. Grahl, and T. G. Parslow, J. Virol. 65:2131-2134,1991; and D. McDonald, T. J. Hope, and T. G. Parslow, J. Virol. 66:7232-7238, 1992).
AB - The RNAs of the hepatitis B virus (HBV) contain a cis-acting regulatory element which facilitates the cytoplasmic localization of unspliced transcripts (J. Huang and T. J. Liang, Mol. Cell. Biol. 13:7476-7486, 1993, and Z. M. Huang and T. S. Yen, J. Virol. 68:3193-3199, 1994). Such localization is presumed to be mediated by cellular factors which interact with the element. The HBV posttranscriptional regulatory element (HBVPRE) can efficiently activate an RNA export reporter system in an orientation-dependent and position-independent manner. Deletion analysis reveals that the HBVPRE consists of two subelements which function synergistically. A synergistic effect was also observed when the 5′ (PREα) or 3′ (PREβ) subelements were duplicated. The bipartite structure of the HBVPRE is reminiscent of reports that the high-affinity binding sites of the Rev-like proteins must be duplicated to function efficiently (M. Grone, E. Hoffmann, S. Berchtold, B. R. Cullen, and R. Grassmann, Virology 204:144-152,1994; X. Huang, T. J. Hope, B. L. Bond, D. McDonald, K. Grahl, and T. G. Parslow, J. Virol. 65:2131-2134,1991; and D. McDonald, T. J. Hope, and T. G. Parslow, J. Virol. 66:7232-7238, 1992).
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U2 - 10.1128/jvi.70.7.4345-4351.1996
DO - 10.1128/jvi.70.7.4345-4351.1996
M3 - Article
C2 - 8676457
AN - SCOPUS:0029903009
SN - 0022-538X
VL - 70
SP - 4345
EP - 4354
JO - Journal of virology
JF - Journal of virology
IS - 7
ER -