It is proposed that the thermally driven motion of certain polypeptide chains, including those that are part of an otherwise stable folded protein, produces timeaveraged three-dimensional domains that confer unique functions to a protein. These domains may be controlled by collapsing the polypeptide
The origins of polypeptide domains
β Scribed by Edward E. Schmidt; Christopher J. Davies
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 206 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0265-9247
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
Three decades ago Gilbert posited that novel proteins arise by reβshuffling genomic sequences encoding polypeptide domains. Today, with numerous genomes and countless genes sequenced, it is well established that recombination of sequences encoding polypeptide domains plays a major role in protein evolution. There is, however, less evidence to suggest how the novel polypeptide domains, themselves, arise. Recent comparisons of genomes from closely related species have revealed numerous speciesβspecific exons, supporting models of domain origin based on βexonizationβ of intron sequences. Also, a mechanism for the origin of novel polypeptide domains has been proposed based on analyses of insertionβbased polymorphisms between orthologous genes across broad phylogenetic spectra and between allelic variants of genes within species. This review discusses these processes and how each might participate in the evolutionary emergence of novel polypeptide domains. BioEssays 29: 262β270, 2007. Β© 2007 Wiley Periodicals, Inc.
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