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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Abstract

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
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 15 Sep 2022 14:31
Last Modified: 23 Sep 2022 02:59
URI: https://ueaeprints.uea.ac.uk/id/eprint/88336
DOI: 10.1139/G10-063

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