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Originally published as Genetics Published Articles Ahead of Print on June 4, 2006.
Genetics, Vol. 173, 1835-1850, August 2006, Copyright © 2006
doi:10.1534/genetics.106.058990
Long-Term Evolution and Functional Diversification in the Members of the Nucleophosmin/Nucleoplasmin Family of Nuclear Chaperones
José M. Eirín-López*,
,
Lindsay J. Frehlick* and
Juan Ausió*,1
* Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada and Departamento de Biología Celular y Molecular, Universidade da Coruña, 15071 A Coruña, Spain
1 Corresponding author: University of Victoria, Department of Biochemistry and Microbiology, Petch Building, Room 220, Victoria, BC V8W 3P6, Canada.
E-mail: jausio{at}uvic.ca
The proper assembly of basic proteins with nucleic acids is a reaction that must be facilitated to prevent protein aggregation and formation of nonspecific nucleoprotein complexes. The proteins that mediate this orderly protein assembly are generally termed molecular (or nuclear) chaperones. The nucleophosmin/nucleoplasmin (NPM) family of molecular chaperones encompasses members ubiquitously expressed in many somatic tissues (NPM1 and -3) or specific to oocytes and eggs (NPM2). The study of this family of molecular chaperones has experienced a renewed interest in the past few years. However, there is a lack of information regarding the molecular evolution of these proteins. This work represents the first attempt to characterize the long-term evolution followed by the members of this family. Our analysis shows that there is extensive silent divergence at the nucleotide level suggesting that this family has been subject to strong purifying selection at the protein level. In contrast to NPM1 and NPM-like proteins in invertebrates, NPM2 and NPM3 have a polyphyletic origin. Furthermore, the presence of selection for high frequencies of acidic residues as well as the existence of higher levels of codon bias was detected at the C-terminal ends, which can be ascribed to the critical role played by these residues in constituting the acidic tracts and to the preferred codon usage for phosphorylatable amino acids at these regions.
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