BETA-GALACTOSIDASE AND SELECTIVE NEUTRALITY

被引:7
作者
HOLMQUIST, R
机构
[1] Space Sciences Laboratory, University of California, Berkeley
关键词
D O I
10.1126/science.106468
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Three hypotheses to explain the amino acid composition of proteins are inconsistent (P ≃ 10-9) with the experimental data for β-galactosidase from Escherichia coli. The exceptional length of this protein, 1021 residues, permits rigorous tests of these hypotheses without complication from statistical artifacts. Either this protein is not at compositional equilibrium, which is unlikely from knowledge about other proteins, or the evolution of this protein and its coding gene have not been selectively neutral. However, the composition of approximately 60 percent of the molecule is consistent with either a selectively neutral or nonneutral evolutionary process. Copyright © 1979 AAAS.
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页码:1012 / 1014
页数:3
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