Plant Physiology Preview
Published on February 24, 2006; 10.1104/pp.105.070672
Received September 29, 2005
Returned for revision November 1, 2005
Accepted January 27, 2006
Calmodulin interacts with and regulates the RNA-binding activity of an Arabidopsis polyadenylation factor subunit
Kim Delaney , Ruqiang Xu , Q. Quinn Li , Kil-Young Yun , Deane L. Falcone , and Arthur G. Hunt *
Department of Plant and Soil Sciences, University of Kentucky, Lexington, KY 40546-0312
Department of Botany, Miami University, Oxford, OH 45056
Department of Biological Sciences, University of Massachusetts, Lowell, MA 01845
* Corresponding author; email: aghunt00{at}uky.edu.
The Arabidopsis gene that encodes the probable orthologue of the 30 kD subunit of the mammalian cleavage and polyadenylation specificity factor (CPSF) is a complex one, encoding small (ca. 28 kD) and large (ca. 68 kD) polypeptides. The small polypeptide (AtCPSF30) corresponds to CPSF30 and is the focus of this study. Recombinant AtCPSF30 was purified from E. coli and found to possess RNA-binding activity. Mutational analysis indicated that an evolutionarily-conserved central core of AtCPSF30 is involved in RNA binding, but that RNA binding also requires a short sequence adjacent to the N-terminus of the central core. AtCPSF30 was found to bind calmodulin, and calmodulin inhibited the RNA-binding activity of the protein in a calcium-dependent manner. Mutational analysis showed that a small part of the protein, again adjacent to the N-terminus of the conserved core, is responsible for calmodulin binding; point mutations in this region abolished both binding to and inhibition of RNA binding by calmodulin. Interestingly, AtCPSF30 was capable of self-interactions. This property also mapped to the central conserved core of the protein. However, calmodulin had no discernible effect on the self-association. These results show that the central portion of AtCPSF30 is involved in a number of important functions, and they raise interesting possibilities for both the interplay between splicing and polyadenylation and the regulation of these processes by stimuli that act through calmodulin.
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