Quantification of the elevated rate of domain rearrangements in metazoa.

@article{citeulike:1978628, abstract = {Most eukaryotic proteins consist of multiple domains created through gene fusions or internal duplications. The most frequent change of a domain architecture (DA) is insertion or deletion of a domain at the N or C terminus. Still, the mechanisms underlying the evolution of multidomain proteins are not very well studied. Here, we have studied the evolution of multidomain architectures (MDA), guided by evolutionary information in the form of a phylogenetic tree. Our results show that Pfam domain families and MDAs have been created with comparable rates (0.1-1 per million years (My)). The major changes in DA evolution have occurred in the process of multicellularization and within the metazoan lineage. In contrast, creation of domains seems to have been frequent already in the early evolution. Furthermore, most of the architectures have been created from older domains or architectures, whereas novel domains are mainly found in single-domain proteins. However, a particular group of exon-bordering domains may have contributed to the rapid evolution of novel multidomain proteins in metazoan organisms. Finally, MDAs have evolved predominantly through insertions of domains, whereas domain deletions are less common. In conclusion, the rate of creation of multidomain proteins has accelerated in the metazoan lineage, which may partly be explained by the frequent insertion of exon-bordering domains into new architectures. However, our results indicate that other factors have contributed as well.}, address = {Stockholm Bioinformatics Center, SCFAB, Stockholm University, SE-10691 Stockholm, Sweden.}, author = {Ekman, D. and Bj\"{o}rklund, A. K. and Elofsson, A. }, citeulike-article-id = {1978628}, doi = {10.1016/j.jmb.2007.06.022}, issn = {0022-2836}, journal = {J Mol Biol}, keywords = {domain, evolution}, month = {October}, number = {5}, pages = {1337--1348}, posted-at = {2007-11-25 09:46:53}, priority = {2}, title = {Quantification of the elevated rate of domain rearrangements in metazoa.}, url = {http://dx.doi.org/10.1016/j.jmb.2007.06.022}, volume = {372}, year = {2007} }

TY - JOUR ID - citeulike:1978628 L3 - citeulike-article-id:1978628 TI - Quantification of the elevated rate of domain rearrangements in metazoa. JF - J Mol Biol VL - 372 IS - 5 SP - 1337 EP - 1348 AD - Stockholm Bioinformatics Center, SCFAB, Stockholm University, SE-10691 Stockholm, Sweden. SN - 0022-2836 N2 - Most eukaryotic proteins consist of multiple domains created through gene fusions or internal duplications. The most frequent change of a domain architecture (DA) is insertion or deletion of a domain at the N or C terminus. Still, the mechanisms underlying the evolution of multidomain proteins are not very well studied. Here, we have studied the evolution of multidomain architectures (MDA), guided by evolutionary information in the form of a phylogenetic tree. Our results show that Pfam domain families and MDAs have been created with comparable rates (0.1-1 per million years (My)). The major changes in DA evolution have occurred in the process of multicellularization and within the metazoan lineage. In contrast, creation of domains seems to have been frequent already in the early evolution. Furthermore, most of the architectures have been created from older domains or architectures, whereas novel domains are mainly found in single-domain proteins. However, a particular group of exon-bordering domains may have contributed to the rapid evolution of novel multidomain proteins in metazoan organisms. Finally, MDAs have evolved predominantly through insertions of domains, whereas domain deletions are less common. In conclusion, the rate of creation of multidomain proteins has accelerated in the metazoan lineage, which may partly be explained by the frequent insertion of exon-bordering domains into new architectures. However, our results indicate that other factors have contributed as well. KW - domain KW - evolution AU - Ekman, D AU - Björklund, AK AU - Elofsson, A PY - 2007/10/05/ UR - http://dx.doi.org/10.1016/j.jmb.2007.06.022 ER -