Low-complexity sequences and single amino acid repeats: Not just "junk" peptide sequences

Haerty, Wilfried ORCID: https://orcid.org/0000-0003-0111-191X and Golding, G. Brian (2010) Low-complexity sequences and single amino acid repeats: Not just "junk" peptide sequences. Genome, 53 (10). pp. 753-762. ISSN 0831-2796

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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.

Item Type: Article
Uncontrolled Keywords: amino acid repeats,selection,simple sequences,biotechnology,molecular biology,genetics ,/dk/atira/pure/subjectarea/asjc/1300/1305
Faculty \ School: Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Medicine and Health Sciences > Research Centres > Norwich Institute for Healthy Aging
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Depositing User: LivePure Connector
Date Deposited: 15 Sep 2022 14:31
Last Modified: 18 Apr 2023 20:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/88336
DOI: 10.1139/G10-063

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