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Inhibition of p53 transactivation function by the human T-cell lymphotropic virus type 1 Tax protein.

Authors
Pise-Massion, CA; Choi, KS; Radonovich, M; Dittmer, J; Kim, SJ; Brady, JN
Citation
Journal of virology, 72(2):1165-1170, 1998
Journal Title
Journal of virology
ISSN
0022-538X1098-5514
Abstract
Human T-cell lymphotropic virus type 1 (HTLV-1) is the etiologic agent for adult T-cell leukemia. HTLV-1 transforms lymphocytes, and there is increasing evidence that the virus-encoded protein, Tax, plays a primary role in viral transformation. We have shown that wild-type p53 in HTLV-1-transformed cells is stabilized. This study was initiated to directly analyze whether the p53 in HTLV-1-transformed cell lines was transcriptionally active and to identify the viral gene product responsible for stabilization and inactivation. Transfection experiments using a p53-responsive reporter plasmid and gamma-irradiation studies demonstrate that the wild-type p53 in HTLV-1-transformed cell lines is not fully active. Further, we demonstrate that the HTLV-1-transforming protein, Tax, stabilizes and inactivates p53 function. Cotransfection of Tax with p53 results in a greater than 10-fold reduction in p53 transcription activity. Using Ga14-p53 fusion proteins, we demonstrate that Tax inhibition of p53 transactivation function is independent of sequence-specific DNA binding. Moreover, Tax inhibits p53 function by interfering with the activity of the N-terminal activation domain (amino acids 1 to 52). We conclude that Tax is involved in the inactivation of p53 function and stabilization of p53 in HTLV-1-infected cells. The functional interference of p53 function by Tax may be important for transformation and leukemogenesis.
MeSH terms
Cell Line, TransformedCell Transformation, Viral/*genetics*Gene Expression Regulation, ViralGene Products, tax/*geneticsHuman T-lymphotropic virus 1/*geneticsHumansTranscriptional ActivationTumor Suppressor Protein p53/*genetics
PMID
9445014
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Biochemistry & Molecular Biology
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