Received date: 2013-11-19
Revised date: 2013-12-20
Online published: 2014-03-26
Ribonuclease A (RNASE A) superfamily is one of the model systems for studying new gene origin and functional innovations in evolutionary biology. Remarkably, gene duplications have been found in many members of RNASE A superfamily, and the functional differentiations of the duplicated genes have been demonstrated to be driven by the adaptive (positive) selection. In this review, we summarize the researches on the evolutionary patterns of RNASE A genes in differ-ent species, especially the recent researches at the genomic levels, suggesting a far more complex and intriguing evolution-ary diversity of RNASE A than previously thought. In the future, along with the increasing numbers of animal genomes available, the studies of RNASE A from more species are expected to reveal new evolutionary patterns and functional di-versifications, which will lay a foundation for the systematic studies on the molecular basis of adaptive evolution.
Datian Lang, Yaping Zhang, Li Yu . Molecular evolution of the ribonuclease A superfamily[J]. Hereditas(Beijing), 2014 , 36(4) : 316 -326 . DOI: 10.3724/SP.J.1005.2014.0316
[1] Kleineidam RG, Pesole G, Breukelman HJ, Beintema JJ, Kastelein RA. Inclusion of cetaceans within the order Artiodactyla based on phylogenetic analysis of pancreatic ribonuclease genes. J Mol Evol, 1999, 48(3): 360–368. <\p>
[2] Wheeler TT, Maqbool NJ, Gupta SK. Mapping, phylogenetic and expression analysis of the RNase (RNaseA) locus in cattle. J Mol Evol, 2012, 74(5–6): 237–248. <\p>
[3] Zhang J. Evolution by gene duplication: an update. Trends Ecology Evol, 2003, 18(6): 292–298. <\p>
[4] Ota T, Nei M. Divergent evolution and evolution by the birth-and-death process in the immunoglobulin VH gene family. Mol Biol Evol, 1994, 11(3): 469–482. <\p>
[5] Makova KD, Li WH. Divergence in the spatial pattern of gene expression between human duplicate genes. Genome Res, 2003, 13(7): 1638–1645. <\p>
[6] Kondrashov FA. Gene duplication as a mechanism of genomic adaptation to a changing environment. Proc Biol Sci, 2012, 279(1749): 5048–5057. <\p>
[7] Magadum S, Banerjee U, Murugan P, Gangapur D, Ravikesavan R. Gene duplication as a major force in evolution. J Genet, 2013, 92(1): 155–161. <\p>
[8] Beintema JJ, Kleineidam RG. The ribonuclease A superfamily: general discussion. Cell Mol Life Sci, 1998, 54(8): 825–832. <\p>
[9] Cho S, Beintema JJ, Zhang J. The ribonuclease A superfamily of mammals and birds: identifying new members and tracing evolutionary histories. Genomics, 2005, 85(2): 208–220. <\p>
[10] Goo SM, Cho S. The expansion and functional diversification of the mammalian ribonuclease A superfamily epitomizes the efficiency of multigene families at generating biological novelty. Genome Biol Evol, 2013, 5(11): 2124–2140. <\p>
[11] Barnard EA. Biological function of pancreatic ribonuclease. Nature, 1969, 221(5178): 340–344. <\p>
[12] Strydom DJ, Fett JW, Lobb RR, Alderman EM, Bethune JL, Riordan JF, Vallee BL. Amino acid sequence of human tumor derived angiogenin. Biochemistry, 1985, 24(20): 5486–5494. <\p>
[13] Harder J, Schroder JM. RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin. J Biol Chem, 2002, 277(48): 46779–46784. <\p>
[14] Zhang J, Dyer KD, Rosenberg HF. Human RNase 7: a new cationic ribonuclease of the RNase A superfamily. Nucleic Acids Res, 2003, 31(2): 602–607. <\p>
[15] Zhang J, Dyer KD, Rosenberg HF. RNase 8, a novel RNase A superfamily ribonuclease expressed uniquely in placenta. Nucleic Acids Res, 2002, 30(5): 1169–1175. <\p>
[16] Rosenberg HF. Eosinophil-derived neurotoxin / RNase 2: connecting the past, the present and the future. Curr Pharm Biotechnol, 2008, 9(3): 135–140. <\p>
[17] Rosenberg HF, Ackerman SJ, Tenen DG. Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity. J Exp Med, 1989, 170(1): 163–176. <\p>
[18] Sorrentino S. The eight human "canonical" ribonucleases: molecular diversity, catalytic properties, and special biological actions of the enzyme proteins. FEBS Lett, 2010, 584(11): 2194–2200. <\p>
[19] Gupta SK, Haigh BJ, Griffin FJ, Wheeler TT. The mammalian secreted RNases: mechanisms of action in host defence. Innate Immun, 2013, 19(1): 86–97. <\p>
[20] Dyer KD, Rosenberg HF. The RNase a superfamily: generation of diversity and innate host defense. Mol Divers, 2006, 10(4): 585–597. <\p>
[21] Rosenberg HF. RNase A ribonucleases and host defense: an evolving story. J Leukoc Biol, 2008, 83(5): 1079–1087. <\p>
[22] Pizzo E, D'Alessio G. The success of the RNase scaffold in the advance of biosciences and in evolution. Gene, 2007, 406(1–2): 8–12. <\p>