The ARE (AU-rich element) is a post-transcriptional element controlling both mRNA turnover and translation initiation by primarily inducing poly(A) tail shortening. The mechanisms by which the ARE-associated proteins induce deadenylation are still obscure. One possibility among others would be that an ARE–ARE-BP (ARE-binding protein) complex intervenes in the PABP [poly(A)-binding protein]–poly(A) tail association and facilitates poly(A) tail accessibility to deadenylases. Here, we show by several experimental approaches that AUF1 (AU-rich element RNA-binding protein 1)/hnRNP (heterogeneous nuclear ribonucleoprotein) D, an mRNA-destabilizing ARE-BP, can bind poly(A) sequence in vitro. First, endogenous AUF1 proteins from HeLa cells specifically bound poly(A), independently of PABP. Secondly, using polyadenylated RNA probes, we showed that (i) the four recombinant AUF1 isoforms bind poly(A) as efficiently as PABP, (ii) the AUF1 binding to poly(A) does not change when the polyadenylated probe contains the GM-CSF (granulocyte/macrophage-colony stimulating factor) ARE, suggesting that, in vitro, the AUF1–poly(A) association was independent of the ARE sequence itself. In vitro, the binding of AUF1 isoforms to poly(A) displayed oligomeric and co-operative properties and AUF1 efficiently displaced PABP from the poly(A). Finally, the AUF1 molar concentration in HeLa cytoplasm was only 2-fold lower than that of PABP, whereas in the nucleus, its molar concentration was similar to that of PABP. These in vitro results suggest that, in vivo, AUF1 could compete with PABP for the binding to poly(A). Altogether, our results may suggest a role for AUF1 in controlling PABP–poly(A) tail association.
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Research Article|
November 14 2006
The ARE-associated factor AUF1 binds poly(A) in vitro in competition with PABP
Francis Sagliocco;
Francis Sagliocco
*INSERM, E362, Bordeaux, F-33076 France; Université Victor Segalen Bordeaux 2, Bordeaux, F-33076 France
†IFR66, Bordeaux, F-33076 France
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Benoît Laloo;
Benoît Laloo
*INSERM, E362, Bordeaux, F-33076 France; Université Victor Segalen Bordeaux 2, Bordeaux, F-33076 France
†IFR66, Bordeaux, F-33076 France
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Bertrand Cosson;
Bertrand Cosson
‡CNRS, UMR 6061, Rennes F-35043, France; Université Rennes I, Rennes, F-35043 France
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Laurence Laborde;
Laurence Laborde
*INSERM, E362, Bordeaux, F-33076 France; Université Victor Segalen Bordeaux 2, Bordeaux, F-33076 France
†IFR66, Bordeaux, F-33076 France
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Michel Castroviejo;
Michel Castroviejo
†IFR66, Bordeaux, F-33076 France
§CNRS, UMR 5097, Bordeaux, F-33076 France; Université Victor Segalen Bordeaux 2, Bordeaux, F-33076 France.
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Jean Rosenbaum;
Jean Rosenbaum
*INSERM, E362, Bordeaux, F-33076 France; Université Victor Segalen Bordeaux 2, Bordeaux, F-33076 France
†IFR66, Bordeaux, F-33076 France
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Jean Ripoche;
Jean Ripoche
*INSERM, E362, Bordeaux, F-33076 France; Université Victor Segalen Bordeaux 2, Bordeaux, F-33076 France
†IFR66, Bordeaux, F-33076 France
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Christophe Grosset
Christophe Grosset
1
*INSERM, E362, Bordeaux, F-33076 France; Université Victor Segalen Bordeaux 2, Bordeaux, F-33076 France
†IFR66, Bordeaux, F-33076 France
1To whom correspondence should be addressed (email christophe.grosset@gref.u-bordeaux2.fr).
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Publisher: Portland Press Ltd
Received:
April 03 2006
Accepted Manuscript online:
July 12 2006
Revision Received:
July 25 2006
Accepted:
August 29 2006
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2006
Biochem J (2006) 400 (2): 337–347.
Article history
Received:
April 03 2006
Accepted Manuscript online:
July 12 2006
Revision Received:
July 25 2006
Accepted:
August 29 2006
Citation
Francis Sagliocco, Benoît Laloo, Bertrand Cosson, Laurence Laborde, Michel Castroviejo, Jean Rosenbaum, Jean Ripoche, Christophe Grosset; The ARE-associated factor AUF1 binds poly(A) in vitro in competition with PABP. Biochem J 1 December 2006; 400 (2): 337–347. doi: https://doi.org/10.1042/BJ20060328
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