Purifying selection drives the evolution of surfactant protein C (SP-C) independently of body temperature regulation in mammals

被引:5
作者
Potter, Sally
Orgeig, Sandra [1 ]
Donnellan, Stephen
Daniels, Christopher B.
机构
[1] Univ S Australia, Sch Pharm & Med Sci, Sansom Inst, Adelaide, SA 5001, Australia
[2] Univ Adelaide, Sch Earth & Environm Sci, Discipline Environm Biol, Adelaide, SA 5005, Australia
[3] Univ Adelaide, Sch Earth & Environm Sci, Ctr Evolut Biol & Biodivers, Adelaide, SA 5005, Australia
[4] S Australian Museum, Evolutionary Biol Unit, Adelaide, SA 5000, Australia
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY D-GENOMICS & PROTEOMICS | 2007年 / 2卷 / 02期
基金
澳大利亚研究理事会;
关键词
pulmonary surfactant; surfactant protein C; mammalian evolution; heterothermy; phylogenetic analysis by maximum likelihood; positive selection;
D O I
10.1016/j.cbd.2007.02.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The pulmonary surfactant system of heterothermic mammals must be capable of dealing with the effect of low body temperatures on the physical state of the lipid components. We have shown previously that there is a modest increase in surfactant cholesterol during periods of torpor, however these changes do not fully explain the capacity of surfactant to function under the wide range of physical conditions imposed by torpor. Here we examine indirectly the role of surfactant protein C (SP-C) in adapting to variable body temperatures by testing for the presence of positive (adaptive) selection during evolutionary transitions between heterothermy and homeothermy. We sequenced SP-C from genomic DNA of 32 mammalian species from groups of closely related heterothermic and homeothermic species (contrasts). We used phylogenetic analysis by maximum likelihood estimates of rates of non-synonymous to synonymous substitutions and fully Bayesian inference of these sequences to determine whether the mode of body temperature regulation exerts a selection pressure driving the molecular adaptation of SP-C. The protein sequence of SP-C is highly conserved with synonymous or highly conservative amino acid substitutions being predominant. The evolution of SP-C among mammals is characterised by high codon usage bias and high rates of transition/transversion. The only contrast to show evidence of positive selection was that of the bears (Ursits atnericanus and U maritimus). The significance of this result is unclear. We show that SP-C is under strong evolutionary constraints, driven by purifying selection, presumably to maintain protein function despite variation in the mode of body temperature regulation. (c) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:165 / 176
页数:12
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