NDLI: Thymidylate Synthase Protein and p53 mRNA Form an In Vivo Ribonucleoprotein Complex

Content Provider	PubMed Central
Author	Chu, Edward Copur, Sitki M. Ju, Jingfang Chen, Tian-men Samir, Khleif Voeller, Donna M. Mizunuma, Nobuyuki Patel, Mahendra Maley, Gladys F. Maley, Frank Allegra, Carmen J.
Copyright Year	1999
Abstract	A thymidylate synthase (TS)-ribonucleoprotein (RNP) complex composed of TS protein and the mRNA of the tumor suppressor gene p53 was isolated from cultured human colon cancer cells. RNA gel shift assays confirmed a specific interaction between TS protein and the protein-coding region of p53 mRNA, and in vitro translation studies demonstrated that this interaction resulted in the specific repression of p53 mRNA translation. To demonstrate the potential biological role of the TS protein-p53 mRNA interaction, Western immunoblot analysis revealed nearly undetectable levels of p53 protein in TS-overexpressing human colon cancer H630-R10 and rat hepatoma H35(F/F) cell lines compared to the levels in their respective parent H630 and H35 cell lines. Polysome analysis revealed that the p53 mRNA was associated with higher-molecular-weight polysomes in H35 cells compared to H35(F/F) cells. While the level of p53 mRNA expression was identical in parent and TS-overexpressing cell lines, the level of p53 RNA bound to TS in the form of RNP complexes was significantly higher in TS-overexpressing cells. The effect of TS on p53 expression was also investigated with human colon cancer RKO cells by use of a tetracycline-inducible system. Treatment of RKO cells with a tetracycline derivative, doxycycline, resulted in 15-fold-induced expression of TS protein and nearly complete suppression of p53 protein expression. However, p53 mRNA levels were identical in transfected RKO cells in the absence and presence of doxycycline. Taken together, these findings suggest that TS regulates the expression of p53 at the translational level. This study identifies a novel pathway for regulating p53 gene expression and expands current understanding of the potential role of TS as a regulator of cellular gene expression.
Starting Page	1582
File Format	PDF
ISSN	10985549
e-ISSN	10985549
Journal	Molecular and Cellular Biology
Issue Number	2
Volume Number	19
Language	English
Publisher	American Society for Microbiology
Publisher Date	1999-02-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Identification of a thymidylate synthase ribonucleoprotein complex in human colon cancer cells.

Control of thymidylate synthase mRNA content and gene transcription in an overproducing mouse cell line.

Analysis of mRNA recognition by human thymidylate synthase

Archaeal Pyrococcus furiosus thymidylate synthase 1 is an RNA-binding protein

RNA–protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex

Ribonucleoprotein complex formation during pre-mRNA splicing in vitro.

Essential Protein-Protein Interactions between Plasmodium falciparum Thymidylate Synthase and Dihydrofolate Reductase Domains*

Apoptosis of haematopoietic cells upon thymidylate synthase inhibition is independent of p53 accumulation and CD95-CD95 ligand interaction.

Coilin Can Form a Complex with the U7 Small Nuclear Ribonucleoprotein

Thymidylate Synthase Protein and p53 mRNA Form an In Vivo Ribonucleoprotein Complex

Similar Documents

Identification of a thymidylate synthase ribonucleoprotein complex in human colon cancer cells.

Control of thymidylate synthase mRNA content and gene transcription in an overproducing mouse cell line.

Analysis of mRNA recognition by human thymidylate synthase

Archaeal Pyrococcus furiosus thymidylate synthase 1 is an RNA-binding protein

RNA–protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex

Ribonucleoprotein complex formation during pre-mRNA splicing in vitro.

Essential Protein-Protein Interactions between Plasmodium falciparum Thymidylate Synthase and Dihydrofolate Reductase Domains*

Apoptosis of haematopoietic cells upon thymidylate synthase inhibition is independent of p53 accumulation and CD95-CD95 ligand interaction.

Coilin Can Form a Complex with the U7 Small Nuclear Ribonucleoprotein

Thymidylate Synthase Protein and p53 mRNA Form an In Vivo Ribonucleoprotein Complex