scholarly journals An extra double-stranded RNA binding domain confers high activity to a squid RNA editing enzyme

RNA ◽  
2009 ◽  
Vol 15 (6) ◽  
pp. 1208-1218 ◽  
Author(s):  
J. P. Palavicini ◽  
M. A. O'connell ◽  
J. J.C. Rosenthal
2012 ◽  
Vol 287 (21) ◽  
pp. 17754-17764 ◽  
Author(s):  
Juan Pablo Palavicini ◽  
Rodrigo A. Correa-Rojas ◽  
Joshua J. C. Rosenthal

2001 ◽  
Vol 12 (7) ◽  
pp. 1911-1924 ◽  
Author(s):  
Christian R. Eckmann ◽  
Andrea Neunteufl ◽  
Lydia Pfaffstetter ◽  
Michael F. Jantsch

The RNA-editing enzyme ADAR1 (adenosine deaminase that acts on RNA) is a bona fide nuclear enzyme that has been cloned from several vertebrate species. Putative nuclear localization signals (NLSs) have been identified in the aminoterminal regions of both human andXenopus ADAR1. Here we show that neither of these predicted NLSs is biologically active. Instead, we could identify a short basic region located upstream of the RNA-binding domains ofXenopus ADAR1 to be necessary and sufficient for nuclear import. In contrast, the homologous region in human ADAR1 does not display NLS activity. Instead, we could map an NLS in human ADAR1 that overlaps with its third double-stranded RNA-binding domain. Interestingly, the NLS activity displayed by this double-stranded RNA-binding domain does not depend on RNA binding, therefore showing a dual function for this domain. Furthermore, nuclear accumulation of human (hs) ADAR1 is transcription dependent and can be stimulated by LMB, an inhibitor of Crm1-dependent nuclear export, indicating that hsADAR1 can move between the nucleus and cytoplasm. Regulated nuclear import and export of hsADAR1 can provide an excellent mechanism to control nuclear concentration of this editing enzyme thereby preventing hyperediting of structured nuclear RNAs.


1995 ◽  
Vol 15 (1) ◽  
pp. 358-364 ◽  
Author(s):  
S R Green ◽  
L Manche ◽  
M B Mathews

The RNA-binding domain of the protein kinase DAI, the double-stranded RNA inhibitor of translation, contains two repeats of a motif that is also found in a number of other RNA-binding proteins. This motif consists of 67 amino acid residues and is predicted to contain a positively charged alpha helix at its C terminus. We have analyzed the effects of equivalent single amino acid changes in three conserved residues distributed over each copy of the motif. Mutants in the C-terminal portion of either repeat were severely defective, indicating that both copies of the motif are essential for RNA binding. Changes in the N-terminal and central parts of the motif were more debilitating if they were made in the first motif than in the second, suggesting that the first motif is the more important for RNA binding and that the second motif is structurally more flexible. When the second motif was replaced by a duplicate of the first motif, the ectopic copy retained its greater sensitivity to mutation, implying that the two motifs have distinct functions with respect to the process of RNA binding. Furthermore, the mutations have the same effect on the binding of double-stranded RNA and VA RNA, consistent with the existence of a single RNA-binding domain for both activating and inhibitory RNAs.


FEBS Journal ◽  
2007 ◽  
Vol 274 (14) ◽  
pp. 3715-3727 ◽  
Author(s):  
Takashi Tadokoro ◽  
Hyongi Chon ◽  
Yuichi Koga ◽  
Kazufumi Takano ◽  
Shigenori Kanaya

2009 ◽  
Vol 284 (38) ◽  
pp. 25471-25478 ◽  
Author(s):  
Jean-Baptiste Marq ◽  
Stéphane Hausmann ◽  
Jeremy Luban ◽  
Daniel Kolakofsky ◽  
Dominique Garcin

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