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Mol Biol Evol. 2006 Apr;23(4):734-43. Epub 2006 Jan 23.

Evolution of circular permutations in multidomain proteins.

Author information

1
Division of Bioinformatics, School of Biological Sciences, University of Münster, Schlossplatz 4, Münster, Germany. january@uni-muenster.de

Abstract

Modular rearrangements play an important role in protein evolution. Functional modules, often tantamount to structural domains or smaller fragments, are in many cases well conserved but reoccur in a different order and across many protein families. The underlying genetic mechanisms are gene duplication, fusion, and loss of sequence fragments. As a consequence, the sequential order of domains can be inverted, leading to what is known as circularly permutated proteins. Using a recently developed algorithm, we have identified a large number of such rearrangements and analyzed their evolutionary history. We searched for examples which have arisen by one of the three postulated mechanisms: independent fusion/fission, "duplication/deletion," and plasmid-mediated "cut and paste." We conclude that all three mechanisms can be observed, with the independent fusion/fission being the most frequent. This can be partly attributed to highly mobile domains. Duplication/deletion has been found in modular proteins such as peptide synthases.

PMID:
16431849
DOI:
10.1093/molbev/msj091
[Indexed for MEDLINE]

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