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For decades proteins were thought to interact in a "lock and key" system, which led to the definition of a paradigm linking stable three-dimensional structure to biological function. As a consequence, any non-structured peptide was considered to be nonfunctional and to evolve neutrally. Surprisingly, the most commonly shared peptides between eukaryotic proteomes are low-complexity sequences that in most conditions do not present a stable three-dimensional structure. However, because these sequences evolve rapidly and because the size variation of a few of them can have deleterious effects, low-complexity sequences have been suggested to be the target of selection. Here we review evidence that supports the idea that these simple sequences should not be considered just "junk" peptides and that selection drives the evolution of many of them.

Original publication

DOI

10.1139/g10-063

Type

Journal article

Journal

Genome

Publication Date

10/2010

Volume

53

Pages

753 - 762

Keywords

Amino Acid Sequence, Animals, Base Composition, Evolution, Molecular, Genetic Code, Humans, Molecular Sequence Data, Peptide Fragments, Repetitive Sequences, Amino Acid, Sequence Analysis, Protein