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Mol. Cells 2012; 34(5): 495-500

Published online November 30, 2012

https://doi.org/10.1007/s10059-012-0232-x

© The Korean Society for Molecular and Cellular Biology

TIP30 Directly Binds p53 Tumor Suppressor Protein In Vitro

Si-Hyung Lee1,2, Sung-Kyu Ju3, Tae-Young Lee4, Sung-Ho Huh2,*, and Kyou-Hoon Han1,5,*

1Biomedical Translational Research Center, Division of Convergent Biomedical Research, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea, 2Department of Biochemistry, Graduate School, Chungnam National University, Daejeon 305-764, Korea, 3Department of Bioscience and Biotechnology, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 305-764, Korea, 4Viral Infectious Disease Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea, 5Department of Bioinformatics, University of Science and Technology, Daejeon 305-333, Korea

Correspondence to : *Correspondence: sungho@cnu.ac.kr (SHH); khhan600@kribb.re.kr (KHH)

Received: September 5, 2012; Revised: October 8, 2012; Accepted: October 9, 2012

Abstract

TIP30 (30 kDa HIV-1 TAT-interacting protein), also called HTATIP2 or CC3, is a tumor suppressor protein that acts as an angiogenesis inhibitor. TIP30 blocks nuclear import of the mRNA-binding protein HuR, and thereby promotes the cytoplasmic accumulation of HuR by binding to im-portin-β, which is known to facilitate the cytoplasm-to-nuclear transport of HuR. Accumulation of HuR in the cytoplasm, in turn, enhances the expression of the transcription factor p53, a tumor suppressor that plays an essential role in preserving genome stability and inhibiting cancer growth. In addition to such a post-transcriptional mechanism via which TIP30 increases the p53 level, it has been proposed that TIP30 may regulate p53 protein at the protein level by directly binding to it. In order to investigate the possibility of direct interaction between p53 and TIP30, we have used on three functional regions in p53 and examined their interactions with TIP30 using GST pull-down assay and surface plasmon resonance technique. The results show that that TIP30 binds to the DNA-binding domain and the C-terminal domain of p53.

Keywords GST pull-down assay, p53, protein-protein interaction, surface plasmon resonance, TIP30

Article

Research Article

Mol. Cells 2012; 34(5): 495-500

Published online November 30, 2012 https://doi.org/10.1007/s10059-012-0232-x

Copyright © The Korean Society for Molecular and Cellular Biology.

TIP30 Directly Binds p53 Tumor Suppressor Protein In Vitro

Si-Hyung Lee1,2, Sung-Kyu Ju3, Tae-Young Lee4, Sung-Ho Huh2,*, and Kyou-Hoon Han1,5,*

1Biomedical Translational Research Center, Division of Convergent Biomedical Research, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea, 2Department of Biochemistry, Graduate School, Chungnam National University, Daejeon 305-764, Korea, 3Department of Bioscience and Biotechnology, College of Biological Sciences and Biotechnology, Chungnam National University, Daejeon 305-764, Korea, 4Viral Infectious Disease Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea, 5Department of Bioinformatics, University of Science and Technology, Daejeon 305-333, Korea

Correspondence to:*Correspondence: sungho@cnu.ac.kr (SHH); khhan600@kribb.re.kr (KHH)

Received: September 5, 2012; Revised: October 8, 2012; Accepted: October 9, 2012

Abstract

TIP30 (30 kDa HIV-1 TAT-interacting protein), also called HTATIP2 or CC3, is a tumor suppressor protein that acts as an angiogenesis inhibitor. TIP30 blocks nuclear import of the mRNA-binding protein HuR, and thereby promotes the cytoplasmic accumulation of HuR by binding to im-portin-β, which is known to facilitate the cytoplasm-to-nuclear transport of HuR. Accumulation of HuR in the cytoplasm, in turn, enhances the expression of the transcription factor p53, a tumor suppressor that plays an essential role in preserving genome stability and inhibiting cancer growth. In addition to such a post-transcriptional mechanism via which TIP30 increases the p53 level, it has been proposed that TIP30 may regulate p53 protein at the protein level by directly binding to it. In order to investigate the possibility of direct interaction between p53 and TIP30, we have used on three functional regions in p53 and examined their interactions with TIP30 using GST pull-down assay and surface plasmon resonance technique. The results show that that TIP30 binds to the DNA-binding domain and the C-terminal domain of p53.

Keywords: GST pull-down assay, p53, protein-protein interaction, surface plasmon resonance, TIP30

Mol. Cells
Sep 30, 2022 Vol.45 No.9, pp. 603~672
COVER PICTURE
The Target of Rapamycin Complex (TORC) is a central regulatory hub in eukaryotes, which is well conserved in diverse plant species, including tomato (Solanum lycopersicum). Inhibition of TORC genes (SlTOR, SlLST8, and SlRAPTOR) by VIGS (virus-induced gene silencing) results in early fruit ripening in tomato. The red/ orange tomatoes are early-ripened TORC-silenced fruits, while the green tomato is a control fruit. Top, left, control fruit (TRV2-myc); top, right, TRV2-SlLST8; bottom, left, TRV2-SlTOR; bottom, right, TRV2-SlRAPTOR(Choi et al., pp. 660-672).

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