Increase of functional diversity by alternative splicing.
A large-scale analysis of protein isoforms arising from alternative splicing shows that alternative splicing tends to insert or delete complete protein domains more frequently than expected by chance, whereas disruption of domains and other structural modules is less frequent. If domain regions are disrupted, the functional effect, as predicted from 3D structure, is frequently equivalent to removal of the entire domain. Also, short alternative splicing events within domains, which might preserve folded structure, target functional residues more frequently than expected. Thus, it seems that positive selection has had a major role in the evolution of alternative splicing.
Kriventseva
Evgenia V
EV
European Bioinformatics Institute (EMBL-EBI), Hinxton Wellcome Trust Genome Campus, Hinxton, Cambridge, UK CB10 1SD.
Koch
Ina
I
Apweiler
Rolf
R
Vingron
Martin
M
Bork
Peer
P
Gelfand
Mikhail S
MS
Sunyaev
Shamil
S
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D019295:Computational Biology; D030562:Databases, Protein; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D020033:Protein Isoforms / Q000032:analysis* / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012641:Selection, Genetic
D000596:Amino Acids; D008024:Ligands; D020033:Protein Isoforms