TY - JOUR
T1 - Did evolution leap to create the protein universe?
AU - Rost, Burkhard
N1 - Funding Information:
Thanks to Jinfeng Liu (Columbia) for computer assistance, for the collection of genome data sets and for providing preliminary data. Also thanks to Henry Bigelow (Columbia) for helpful comments on the manuscript. The work of B Rost was supported by grants 1-P50-GM62413-01 and RO1-GM63029-01 from the National Institutes of Health. Last, but not least, thanks to all those who deposit their experimental data in public databases and to those who maintain these databases. I refrained from quoting older publications, even if these would have been more appropriate; my apologies to those who should have been quoted. In highlighting papers, I considered only original articles and tended to ignore papers describing methods and databases, although these were the basis of the papers that were highlighted.
PY - 2002/6/1
Y1 - 2002/6/1
N2 - The genomes of over 60 organisms from all three kingdoms of life are now entirely sequenced. In many respects, the inventory of proteins used in different kingdoms appears surprisingly similar. However, eukaryotes differ from other kingdoms in that they use many long proteins, and have more proteins with coiled-coil helices and with regions abundant in regular secondary structure. Particular structural domains are used in many pathways. Nevertheless, one domain tends to occur only once in one particular pathway. Many proteins do not have close homologues in different species (orphans) and there could even be folds that are specific to one species. This view implies that protein fold space is discrete. An alternative model suggests that structure space is continuous and that modern proteins evolved by aggregating fragments of ancient proteins. Either way, after having harvested proteomes by applying standard tools, the challenge now seems to be to develop better methods for comparative proteomics.
AB - The genomes of over 60 organisms from all three kingdoms of life are now entirely sequenced. In many respects, the inventory of proteins used in different kingdoms appears surprisingly similar. However, eukaryotes differ from other kingdoms in that they use many long proteins, and have more proteins with coiled-coil helices and with regions abundant in regular secondary structure. Particular structural domains are used in many pathways. Nevertheless, one domain tends to occur only once in one particular pathway. Many proteins do not have close homologues in different species (orphans) and there could even be folds that are specific to one species. This view implies that protein fold space is discrete. An alternative model suggests that structure space is continuous and that modern proteins evolved by aggregating fragments of ancient proteins. Either way, after having harvested proteomes by applying standard tools, the challenge now seems to be to develop better methods for comparative proteomics.
UR - http://www.scopus.com/inward/record.url?scp=0036601151&partnerID=8YFLogxK
U2 - 10.1016/S0959-440X(02)00337-8
DO - 10.1016/S0959-440X(02)00337-8
M3 - Review article
C2 - 12127462
AN - SCOPUS:0036601151
SN - 0959-440X
VL - 12
SP - 409
EP - 416
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 3
ER -