Co-evolution of the branch site and SR proteins in eukaryotes.
Serine-arginine-rich (SR) proteins are essential for splicing in metazoans but are absent in yeast. By contrast, many fungi have SR protein homologs with variable arginine-rich regions analogous to the arginine-serine-rich (RS) domain in metazoans. The density of RS repeats in these regions correlates with the conservation of the branch site signal, providing evidence for an ancestral origin of SR proteins and indicating that the SR proteins and the branch site co-evolved.
Plass
Mireya
M
Computational Genomics Group, Universitat Pompeu Fabra, PRBB, Dr. Aiguader 88 E08003, Barcelona, Spain.
Agirre
Eneritz
E
Reyes
Diana
D
Camara
Francisco
F
Eyras
Eduardo
E
D005057:Eukaryotic Cells / Q000378:metabolism*; D019143:Evolution, Molecular; D005091:Exons / Q000235:genetics; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics*; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012326:RNA Splicing; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000235:genetics*; D000068103:Serine-Arginine Splicing Factors
D009687:Nuclear Proteins; D016601:RNA-Binding Proteins; D000068103:Serine-Arginine Splicing Factors