Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism.
Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.
Liu
Yang
Y
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
Gerstein
Mark
M
Engelman
Donald M
DM
D000818:Animals; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics; D005057:Eukaryotic Cells; D019143:Evolution, Molecular; D014644:Genetic Variation; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics*; D008957:Models, Genetic; D011387:Prokaryotic Cells; D017434:Protein Structure, Tertiary; D011995:Recombination, Genetic
D019843:Archaeal Proteins; D008565:Membrane Proteins