Phylogenetic analyses of amino acid variation in the serpin proteins

被引:35
作者
Atchley, WR
Lokot, T
Wollenberg, K
Dress, A
Ragg, H
机构
[1] N Carolina State Univ, Dept Genet, Raleigh, NC 27695 USA
[2] Univ Bielefeld, Fac Technol, D-4800 Bielefeld, Germany
[3] Univ Bielefeld, Fac Math, D-4800 Bielefeld, Germany
关键词
serpins; molecular evolution; phylogeny; protein evolution; maximum likelihood; neighbor joining;
D O I
10.1093/oxfordjournals.molbev.a003936
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
Phylogenetic analyses of 110 serpin protein sequences revealed clades consistent with independent phylogenetic analyses based on exon-intron structure and diagnostic amino acid sites. Trees were estimated by maximum likelihood, neighbor joining and partial split decomposition using both the BLOSUM 62 and Jones-Taylor-Thornton substitution matrices. Neighbor-joining trees gave results closest to those based on independent analyses using genomic and chromosomal data. The maximum-likelihood trees derived using the quartet puzzling algorithm were very conservative, producing many small clades that separated groups of proteins that other results suggest were related. Independent analyses based on exon-intron structure suggested that a neighbor-joining tree was more accurate than maximum-likelihood trees obtained using the quartet puzzling algorithm.
引用
收藏
页码:1502 / 1511
页数:10
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