Essential role for the interaction between hnRNP H/F and a G quadruplex in maintaining p53 pre-mRNA 3′-end processing and function during DNA damage

被引:141
作者
Decorsiere, Adrien [1 ,2 ,3 ]
Cayrel, Anne [1 ,2 ,3 ]
Vagner, Stephan [1 ,2 ,3 ]
Millevoi, Stefania [1 ,2 ,3 ]
机构
[1] INSERM, U563, F-31000 Toulouse, France
[2] Inst Claudius Regaud, F-31052 Toulouse, France
[3] Univ Toulouse 3, F-31000 Toulouse, France
关键词
DNA damage; pre-mRNA 3 '-end processing; polyadenylation; p53 tumor suppressor; hnRNP H; hnRNP F; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; RIBOSOMAL-PROTEIN L26; MOLECULAR-MECHANISMS; DOWN-REGULATION; POLYMERASE-II; IN-VITRO; TRANSLATION; EXPRESSION; PHOSPHORYLATION; POLYADENYLATION;
D O I
10.1101/gad.607011
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Following DNA damage, mRNA 39-end formation is inhibited, contributing to repression of mRNA synthesis. Here we investigated how DNA-damaged cells accomplish p53 mRNA 39-end formation when normal mechanisms of pre-mRNA 39-end processing regulation are inhibited. The underlying mechanism involves the interaction between a G-quadruplex structure located downstream from the p53 cleavage site and hnRNP H/F. Importantly, this interaction is critical for p53 expression and contributes to p53-mediated apoptosis. Our results uncover the existence of a specific rescue mechanism of 39-end processing regulation allowing stress-induced p53 accumulation and function in apoptosis.
引用
收藏
页码:220 / 225
页数:6
相关论文
共 34 条
[1]   Origins of binding specificity of the A1 heterogeneous nuclear ribonucleoprotein [J].
AbdulMana, N ;
OMalley, SM ;
Williams, KR .
BIOCHEMISTRY, 1996, 35 (11) :3545-3554
[2]   The hnRNPs F and H2 bind to similar sequences to influence gene expression [J].
Alkan, SA ;
Martincic, K ;
Milcarek, C .
BIOCHEMICAL JOURNAL, 2006, 393 (01) :361-371
[3]   DSEF-1 is a member of the hnRNP H family of RNA-binding proteins and stimulates pre-mRNA cleavage and polyadenylation in vitro [J].
Bagga, PS ;
Arhin, GK ;
Wilusz, J .
NUCLEIC ACIDS RESEARCH, 1998, 26 (23) :5343-5350
[4]   Che-1 phosphorylation by ATM/ATR and Chk2 kinases activates p53 transcription and the G2/M checkpoint [J].
Bruno, Tiziana ;
De Nicola, Francesca ;
Iezzi, Simona ;
Lecis, Daniele ;
D'Angelo, Carmen ;
Di Padova, Monica ;
Corbi, Nicoletta ;
Dimiziani, Leopoldo ;
Zannini, Laura ;
Jekimovs, Christian ;
Scarsella, Marco ;
Porrello, Alessandro ;
Chersi, Alberto ;
Crescenzi, Marco ;
Leonetti, Carlo ;
Khanna, Kum Kum ;
Soddu, Silvia ;
Floridi, Aristide ;
Passananti, Claudio ;
Delia, Domenico ;
Fanciulli, Maurizio .
CANCER CELL, 2006, 10 (06) :473-486
[5]   CPEB regulation of human cellular senescence, energy metabolism, and p53 mRNA translation [J].
Burns, David M. ;
Richter, Joel D. .
GENES & DEVELOPMENT, 2008, 22 (24) :3449-3460
[6]   P68 RNA Helicase (DDX5) Alters Activity of Cis- and Trans-Acting Factors of the Alternative Splicing of H-Ras [J].
Camats, Maria ;
Guil, Sonia ;
Kokolo, Mariette ;
Bach-Elias, Montse .
PLOS ONE, 2008, 3 (08)
[7]   Nuclear deadenylation/polyadenylation factors regulate 3′ processing in response to DNA damage [J].
Cevher, Murat A. ;
Zhang, Xiaokan ;
Fernandez, Sully ;
Kim, Sergey ;
Baquero, Jorge ;
Nilsson, Per ;
Lee, Sean ;
Virtanen, Anders ;
Kleiman, Frida E. .
EMBO JOURNAL, 2010, 29 (10) :1674-1687
[8]   Auxiliary downstream elements are required for efficient polyadenylation of mammalian pre-mRNAs [J].
Chen, F ;
Wilusz, J .
NUCLEIC ACIDS RESEARCH, 1998, 26 (12) :2891-2898
[9]   Two G-rich regulatory elements located adjacent to and 440 nucleotides downstream of the core poly(A) site of the intronless melanocortin receptor 1 gene are critical for efficient 3′ end processing [J].
Dalziel, Martin ;
Nunes, Nuno Miguel ;
Furger, Andre .
MOLECULAR AND CELLULAR BIOLOGY, 2007, 27 (05) :1568-1580
[10]   3′ end mRNA processing:: molecular mechanisms and implications for health and disease [J].
Danckwardt, Sven ;
Hentze, Matthias W. ;
Kulozik, Andreas E. .
EMBO JOURNAL, 2008, 27 (03) :482-498