PL EN


Preferences help
enabled [disable] Abstract
Number of results
2016 | 63 | 4 | 645-651
Article title

The role of the 5' terminal region of p53 mRNA in the p53 gene expression

Content
Title variants
Languages of publication
EN
Abstracts
EN
The p53 tumour suppressor protein is one of the major factors responsible for cell cycle regulation and protection against cancer development. This is why it is often referred to as "the guardian of the genome". On the other hand, mutations in the p53 gene are connected with more than 50% of tumours of various types. The thirty-six years of extensive research on the p53 gene and its protein products have shown how sophisticated the p53-based cell system control is. An additional level of complexity of the p53 research is connected with at least twelve p53 isoforms which have been identified in the cell. Importantly, disturbance of the p53 isoforms' expression seems to play a key role in tumorigenesis, cell differentiation and cell response to pathogenic bacteria, and RNA and DNA viruses. Expression of various p53 isoforms results from the usage of different transcription promoters, alternative splicing events and translation initiation from alternative AUG codons. The importance of the 5'-terminal regions of different p53 mRNA transcripts in the multi-level regulation of the p53 gene has recently been documented. In this review we focus on the structural features of these regions and their specific role in the p53 translation initiation process.
Keywords
Publisher

Year
Volume
63
Issue
4
Pages
645-651
Physical description
Dates
published
2016
received
2016-05-31
revised
2016-06-28
accepted
2016-07-13
(unknown)
2016-10-25
Contributors
  • Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznań, Poland
  • Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznań, Poland
author
  • Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznań, Poland
  • Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznań, Poland
References
  • Babendure JR, Babendure JL, Ding JH, Tsien RY (2006) Control of mammalian translation by mRNA structure near caps. RNA 12: 851−861.
  • Baker SJ, Fearon ER, Nigro JM, Hamilton SR, Preisinger AC, Jessup JM, van Tuinen P, Ledbetter DH, Barker DF, Nakamura Y, White R, Vogelstein B (1989) Chromosome 17 deletions and p53 gene mutations in colorectal carcinomas. Science 244: 217-221.
  • Bellodi C, Kopmar N, Ruggero D (2010) Deregulation of oncogene-induced senescence and p53 translational control in X-linked dyskeratosis congenital. EMBO J 29: 1865-1876. https://doi.org/10.1038/emboj.2010.83.
  • Bienz-Tadmor B, Zakut-Houri R, Libresco S, Givol D, Oren M (1985) The 5' region of the p53 gene: evolutionary conservation and evidence for a negative regulatory element. EMBO J 4: 3209-3213.
  • Blaszczyk L, Ciesiolka J (2011) Secondary structure and the role in translation initiation of the 5'-terminal region of p53 mRNA. Biochemistry 50: 7080-7092. https://doi.org/10.1021/bi200659b.
  • Bourdon JC (2007) p53 and its isoforms in cancer. Br J Cancer 97: 277-282.
  • Bourdon JC, Fernandes K, Murray-Zmijewski F, Liu G, Diot A, Xirodimas DP, Saville MK, Lane DP (2005) p53 isoforms can regulate p53 transcriptional activity. Genes Development 19: 2122-2137.
  • Bourougaa K, Naski N, Boularan C, Mlynarczyk C, Candeias MM, Marullo S, Fahraeus R (2010) Endoplasmic reticulum stress induces G2 cell-cycle arrest via mRNA translation of the p53 isoform p53/47. Mol Cell 38: 78-88. https://doi.org/10.1016/j.molcel.2010.01.041.
  • Brooks CL, Gu W (2011) p53 regulation by ubiquitin. FEBS Lett 585: 2803-2809. https://doi.org/10.1016/j.febslet.2011.05.022.
  • Candeias MM, Malbert-Colas L, Powell DJ, Daskalogianni C, Maslon MM, Naski N, Bourougaa K, Calvo F, Fahraeus R (2008) p53 mRNA controls p53 activity by managing Mdm2 functions. Nat Cell Biol 10: 1098-105. https://doi.org/10.1038/ncb1770.
  • Chen J, Kastan MB (2010) 5'-3'-UTR interactions regulate p53 mRNA translation and provide a target for modulating p53 induction after DNA damage. Genes Dev 24: 2146-56. https://doi.org/10.1101/gad.1968910.
  • Christian KJ, Lang MA, Raffalli-Mathieu F (2008) Interaction of heterogeneous nuclear ribonucleoprotein C1/C2 with a novel cis-regulatory element within p53 mRNA as a response to cytostatic drug treatment. Mol Pharmacol 73: 1558-1567. https://doi.org/10.1124/mol.107.042507.
  • Courtois S, Verhaegh G, North S, Luciani MG, Lassus P, Hibner U, Oren M, Hainaut P (2002) DeltaN-p53, a natural isoform of p53 lacking the first transactivation domain, counteracts growth suppression by wild-type p53. Oncogene 21: 6722-6728.
  • Farnebo M (2009) Wrap53, a novel regulator of p53. Cell Cycle 8: 2343-2346.
  • Fitzgerald KD, Semler BL (2009) Bridging IRES elements in mRNAs to the eukaryotic translation apparatus. Biochim Biophys Acta 1789: 518-528. https://doi.org/10.1016/j.bbagrm.2009.07.004.
  • Gallego J (2002) Internal initiation of translation by viral and cellular IRESs - a new avenue for specific inhibition of protein synthesis? Curr Opin Drug Discov Devel 5: 777-784.
  • Ghosh A, Stewart D, Matlashewski G. (2004) Regulation of human p53 activity and cell localization by alternative splicing. Mol Cell Biol 24: 7987-7997.
  • Górska A, Błaszczyk L, Dutkiewicz M, Ciesiołka J (2013) Length variants of the 5' untranslated region of p53 mRNA and their impact on the efficiency of translation initiation of p53 and its N-truncated isoform ΔNp53. RNA Biology 10: 1726-1740. https://doi.org/10.4161/rna.26562.
  • Grover R, Candeias MM, Fahraeus R, Das S (2009) p53 and little brother p53/47: linking IRES activities with protein functions. Oncogene 28: 2766-2772. https://doi.org/10.1038/onc.2009.138.
  • Grover R, Ray PS, Das S (2008) Polypyrimidine tract binding protein regulates IRES-mediated translation of p53 isoforms. Cell Cycle 7: 2189-2198.
  • Grover R, Sharathchandra A, Ponnuswamy A, Khan D, Das S (2011) Effect of mutations on the p53 IRES RNA structure: implications for de-regulation of the synthesis of p53 isoforms. RNA Biol 8: 132-142.
  • Haley B, Paunesku T, Protic M, Woloschak GE (2009) Response of heterogeneous ribonuclear proteins (hnRNP) to ionising radiation and their involvement in DNA damage repair. Int J Radiat Biol 85: 643-655. https://doi.org/10.1080/09553000903009548.
  • Khan D, Katoch A, Das A, Sharathchandra A, Lal R, Roy P, Chattopadhyay S, Das S (2015) Reversible induction of translational isoforms of p53 in glucose deprivation. Cell Death Differ 22: 1203-1218. https://doi.org/10.1038/cdd.2014.220.
  • Khan D, Sharathchandra A, Ponnuswamy A, Grover R, Das S (2013) Effect of a natural mutation in the 5' untranslated region on the translational control of p53 mRNA. Oncogene 32: 4148-4159. https://doi.org/10.1038/onc.2012.422.
  • Khoury MP, Bourdon JC (2010) The isoforms of the p53 protein. Cold Spring Harb Perspect Biol 2: a000927.
  • Khoury MP, Bourdon JC (2011) p53 Isoforms: An Intracellular Microprocessor? Genes Cancer 2: 453-465. https://doi.org/10.1177/1947601911408893.
  • Kozak M (1989) Circumstances and mechanisms of inhibition of translation by secondary structure in eukaryotic mRNAs. Mol Cell Biol 9: 5134-5142.
  • Kozak M (2005) Regulation of translation via mRNA structure in prokaryotes and eukaryotes. Gene 361: 13-37.
  • Lamb P, Crawford L (1986) Characterization of the human p53 gene. Mol Cell Biol 6: 1379-1385.
  • Lane D, Crawford L (1979) T antigen is bound to a host protein in SV40-transformed cells. Nature 278: 261-263.
  • Lankat-Buttgereit B, Goke R (2009) The tumour suppressor Pdcd4: recent advances in the elucidation of function and regulation. Biol Cell 101: 309-17. https://doi.org/10.1042/BC20080191.
  • Linzer DI, Maltzman W, Levine AJ (1979) The SV40 A gene product is required for the production of a 54 000 MW cellular tumor antigen. Virology 98: 308-318.
  • Mahmoudi S, Henriksson S, Corcoran M, Mendez-Vidal C, Wiman KG, Farnebo M (2009) Wrap53, a natural p53 antisense transcript required for p53 induction upon DNA damage. Mol Cell 33: 462-471. https://doi.org/10.1016/j.molcel.2009.01.028.
  • Marcel V, Dichtel-Danjoy ML, Sagne C, Hafsi H, Ma D, Ortiz-Cuaran S, Olivier M, Hall J, Mollereau B, Hainaut P, Bourdon JC (2011) Biological functions of p53 isoforms through evolution: lessons from animal and cellular models, Cell Death and Differentiation 18: 1815-1824. https://doi.org/10.1038/cdd.2011.120.
  • Marcel V, Perrier S, Aoubala M, Ageorges S, Groves MJ, Diot A, Fernandes K, Tauro S, Bourdon JC (2010) Δ160p53 is a novel N-terminal p53 isoform encoded by Δ133p53 transcript. FEBS Lett 584: 4463-4468. https://doi.org/10.1016/j.febslet.2010.10.005.
  • Marcel V, Hainaut P (2009) p53 isoforms - a conspiracy to kidnap p53 tumor suppressor activity? Cell Mol Life Sci 66: 391-406. https://doi.org/10.1007/s00018-008-8336-3.
  • Muller PA, Vousden KH (2013) p53 mutations in cancer. Nature Cell Biol 15: 2-8. https://doi.org/10.1038/ncb2641.
  • Olivares-Illana V, Fahraeus R (2010) p53 isoforms gain functions. Oncogene 29: 5113-5119. https://doi.org/10.1038/onc.2010.266.
  • Powell DJ, Hrstka R, Candeias M, Bourougaa K, Vojtesek B, Fahraeus R (2008) Stress-dependent changes in the properties of p53 complexes by the alternative translation product p53/47. Cell Cycle 7: 950-959.
  • Ray PS, Grover R, Das S (2006) Two internal ribosome entry sites mediate the translation of p53 isoforms. EMBO Reports 7: 404-410.
  • Reisman D, Greenberg M, Rotter V (1988) Human p53 oncogene contains one promoter upstream of exon 1 and a second, stronger promoter within intron 1. Proc Natl Acad Sci U S A 85: 5146-5150.
  • Sawicka K, Bushell M, Spriggs KA, Willis AE (2008) Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein. Biochem Soc Trans 36: 641-647. https://doi.org/10.1042/BST0360641.
  • Schellenberg MJ, Ritchie DB, MacMillan AM (2008) Pre-mRNA splicing: a complex picture in higher definition. Trends Biochem Sci 33: 243-246. https://doi.org/10.1016/j.tibs.2008.04.004.
  • Sharathchandra A, Lal R, Khan D, Das S (2012) Annexin A2 and PSF proteins interact with p53 IRES and regulate translation of p53 mRNA. RNA Biol 9: 1429-1439. https://doi.org/10.4161/rna.22707.
  • Sonenberg N, Hinnebusch AG (2009) Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136: 731-745. https://doi.org/10.1016/j.cell.2009.01.042.
  • Strudwick S, Carastro LM, Stagg T, Lazarus P (2003) Differential transcription-coupled translational inhibition of human p53 expression: a potentially important mechanism of regulating p53 expression in normal versus tumor tissue. Mol Cancer Res 1: 463-474.
  • Swiatkowska A, Zydowicz P, Gorska A, Suchacka J, Dutkiewicz M, Ciesiołka J (2015) The role of structural elements of the 5'-terminal region of p53 mRNA in translation under stress conditions assayed by the antisense oligonucleotide approach. PLoS One 10: e0141676. https://doi.org/10.1371.
  • Takagi M, Absalon MJ, McLure KG, Kastan MB (2005) Regulation of p53 translation and induction after DNA damage by ribosomal protein L26 and nucleolin. Cell 123: 49-63.
  • Terrier O, Bourdon JC, Rosa-Calatrava M (2013) p53 protein isoforms: key regulators in the front line of pathogen infections? PLOS Pathogens 9: e1003246.
  • Tuck SP, Crawford L (1989) Characterization of the human p53 gene promoter. Mol Cell Biol 9: 2163-2172.
  • Ungewitter E, Scrable H (2010) Δ40p53 controls the switch from pluripotency to differentiation by regulating IGF signaling in ESCs. Genes and Development 24: 2408-2419. https://doi.org/10.1101/gad.1987810.
  • Vassilenko KS, Alekhina OM, Dmitriev SE, Shatsky IN, Spirin AS (2011) Unidirectional constant rate motion of the ribosomal scanning particle during eukaryotic translation initiation Nucleic Acids Res 39: 5555-5567. https://doi.org/10.1093/nar/gkr147.
  • Wang Z, Li B (2010) Mdm2 links genotoxic stress and metabolism to p53. Protein Cell 1: 1063-1072. https://doi.org/10.1007/s13238-010-0140-9.
  • Wedeken L, Singh P, Klempnauer KH (2011) Tumor suppressor protein Pdcd4 inhibits translation of p53 mRNA. J Biol Chem 286: 42855-42862. https://doi.org/10.1074/jbc.M111.269456.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv63p645kz
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.