Abstract
The evolution of complex genomes requires that new combinations of pre-existing protein domains successfully fold into modular polypeptides. During eukaryotic translation model two-domain polypeptides fold efficiently by sequential and co-translational folding of their domains. In contrast, folding of the same proteins in Escherichia coli is posttranslational, and leads to intramolecular misfolding of concurrently folding domains. Sequential domain folding in eukaryotes may have been critical in the evolution of modular polypeptides, by increasing the probability that random gene-fusion events resulted in immediately foldable protein structures.
MeSH terms
-
Animals
-
Bacterial Proteins / genetics
-
Bacterial Proteins / metabolism
-
Binding Sites
-
Cloning, Molecular
-
Cytosol / metabolism
-
Escherichia coli / genetics
-
Escherichia coli / metabolism
-
Eukaryotic Cells / metabolism
-
Evolution, Molecular
-
Humans
-
Mice
-
Protein Biosynthesis*
-
Protein Folding*
-
Protein Processing, Post-Translational
-
Recombinant Fusion Proteins / metabolism
-
Recombination, Genetic*
-
Ribosomes / metabolism
-
Tetrahydrofolate Dehydrogenase / genetics
-
Tetrahydrofolate Dehydrogenase / metabolism
-
Transcription Factors / genetics
-
Transcription Factors / metabolism
-
ras Proteins / genetics
-
ras Proteins / metabolism
Substances
-
Bacterial Proteins
-
Recombinant Fusion Proteins
-
Transcription Factors
-
Tetrahydrofolate Dehydrogenase
-
ras Proteins