Selective pressures that decrease synonymous mutations in Plasmodium falciparum.
Rich and Ayala propose that the zero rate of non-amino-acid-changing (synonymous) mutations in some proteins of Plasmodium falciparum reflects a recent population bottleneck. Alternatively, Arnot and Saul propose sequence conservation in response to selective pressures other than the pressure to encode protein. Among these are fold pressure and purine-loading pressure. Genomes adapt to these by acquisition of introns and/or low-complexity (simple-sequence) segments in proteins. Adaptive explanations include facilitation of intragenic recombination (and hence diversification of the encoded protein) by DNA stem-loop secondary structures.
Forsdyke
Donald R
DR
Dept of Biochemistry, Queen's University, Kingston, Ontario, Canada K7L3N6. forsdyke@post.queensu.ca
D000595:Amino Acid Sequence / Q000235:genetics; D000818:Animals; D000953:Antigens, Protozoan / Q000235:genetics; D001482:Base Composition; D001483:Base Sequence / Q000235:genetics; D019143:Evolution, Molecular; D004854:Herpesvirus 4, Human / Q000235:genetics; D010963:Plasmodium falciparum / Q000235:genetics*; D017354:Point Mutation / Q000235:genetics*; D017510:Protein Folding; D015800:Protozoan Proteins / Q000235:genetics; D012641:Selection, Genetic
D000953:Antigens, Protozoan; D015800:Protozoan Proteins; C041595:circumsporozoite protein, Protozoan; C065974:merozoite surface protein 2, Plasmodium