Year: 2019
Type: article
Abstract: Low complexity regions (LCRs) in protein sequences have special properties that are very different from those of globular proteins. The rules that define secondary structure elements do not apply when the distribution of amino acids becomes biased. While there is a tendency towards structural disorder in LCRs, various examples, and particularly homorepeats of single amino acids, suggest that very short repeats could adopt structures very difficult to predict. These structures are possibly variable and dependant on the context of intra- or inter-molecular interactions. In general, short repeats in LCRs can induce structure. This could explain the observation that very short (non-perfect) repeats are widespread and many define regions with a function in protein interactions. For these reasons, we have developed an algorithm to quickly analyze local repeatability along protein sequences, that is, how close a protein fragment is from a perfect repeat. Using this algorithm we identified that the proteins of the yeast Saccharomyces cerevisiae are depleted in short repeats (approximate or not) of odd-length, while the human proteins are not, that the fish Danio rerio has many proteins with repeats of length two and that the plant Arabidopsis thaliana has an unusually large amount of repeats of length seven. Our method (REpeatability Scanner, RES, accessible at http://cbdm-01.zdv.uni-mainz.de/~munoz/res/) allows to find regions with approximate short repeats in protein sequences, and helps to characterize the variable use of LCRs and compositional bias in different organisms.
Source: Journal of Structural Biology
Authors: Mohamed Kamel, Pablo Mier, Abdelkamel Tari, Miguel A. Andrade-Navarro
Institutions: University of Béjaïa, Johannes Gutenberg University Mainz
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $2,750
Funder: Deutsche Forschungsgemeinschaft
Award: G2258699807
OpenAlex ID: W2967567705