Extensive amino acid polymorphism at the pgm locus is consistent with adaptive protein evolution in Drosophila melanogaster.
Extensive amino acid polymorphism at the pgm locus is consistent with adaptive protein evolution in Drosophila melanogaster.
复制标题
pgm 位点的广泛氨基酸多态性与果蝇的适应性蛋白质进化一致。
DOI:
10.1093/genetics/156.4.1737
复制
发表时间:
2000
期刊:
影响因子:
3.3
通讯作者:
Eanes,WF
中科院分区:
文献类型:
--
作者:
Verrelli,BC;Eanes,WF
PGM plays a central role in the glycolytic pathway at the branch point leading to glycogen metabolism and is highly polymorphic in allozyme studies of many species. We have characterized the nucleotide diversity across thePgmgene inDrosophila melanogasterandD. simulansto investigate the role that protein polymorphism plays at this crucial metabolic branch point shared with several other enzymes. AlthoughD. melanogasterandD. simulansshare common allozyme mobility alleles, we find these allozymes are the result of many different amino acid changes at the nucleotide level. In addition, specific allozyme classes within species contain several amino acid changes, which may explain the absence of latitudinal clines for PGM allozyme alleles, the lack of association of PGM allozymes with the cosmopolitanIn(3L)Pinversion, and the failure to detect differences between PGM allozymes in functional studies. We find a significant excess of amino acid polymorphisms withinD. melanogasterwhen compared to the complete absence of fixed replacements withD. simulans.There is also strong linkage disequilibrium across the 2354 bp of thePgmlocus, which may be explained by a specific amino acid haplotype that is high in frequency yet contains an excess of singleton polymorphisms. LikeG6pd, Pgmshows strong evidence for a branch point enzyme that exhibits adaptive protein evolution.