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p27x-III and p21x-III, proteins encoded by the pX sequence of human T-cell leukemia virus type I.
Author(s) -
Tetsuyuki Kiyokawa,
Motoharu Seiki,
Shintaro Iwashita,
K Imagawa,
Fumio Shimizu,
Mitsuzi Yoshida
Publication year - 1985
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.24.8359
Subject(s) - phosphoprotein , open reading frame , microbiology and biotechnology , biology , gene , virology , peptide sequence , t cell , leukemia , cell culture , gene product , virus , murine leukemia virus , gene expression , genetics , immune system
Human T-cell leukemia virus type I (HTLV-I) is an etiological agent of adult T-cell leukemia and has a unique sequence, pX, that contains four possible open reading frames, I-IV. p40x was previously identified as the gene product of frame IV (x-lor) and was suggested to mediate transcriptional trans-activation of the viral long terminal repeats. We have identified two pX gene products, p27x-III and p21x-III, encoded by frame III, which mostly overlapped frame IV. These proteins were detected with rabbit antiserum against the synthetic peptide predicted from the 3' end of frame III. p27x-III is phosphorylated in cultured cells, and the phosphoprotein (pp27x-III) is localized in nuclei; some pp27x-III was tightly bound to nuclear components. p27x-III was detected in a number of cell lines that express other viral antigens, including a cell line previously reported to express only p40x as a viral protein. The function(s) of p27x-III and p21x-III is not known, but the tight binding of pp27x-III to nuclear components suggests that it is associated with regulation of viral gene expression.

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