Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon bias

A significant number of proteins in all living species contains amino acid repeats (AARs) of various lengths and compositions, many of which play important roles in protein structure and function. Here, I have surveyed select homopolymeric single [(A)n] and double [(AB)n] AARs in the human proteome....

Full description

Bibliographic Details
Main Author: Sailen Barik
Format: Article
Language:English
Published: Elsevier 2017-12-01
Series:Heliyon
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S240584401733548X
_version_ 1811204256873578496
author Sailen Barik
author_facet Sailen Barik
author_sort Sailen Barik
collection DOAJ
description A significant number of proteins in all living species contains amino acid repeats (AARs) of various lengths and compositions, many of which play important roles in protein structure and function. Here, I have surveyed select homopolymeric single [(A)n] and double [(AB)n] AARs in the human proteome. A close examination of their codon pattern and analysis of RNA structure propensity led to the following set of empirical rules: (1) One class of amino acid repeats (Class I) uses a mixture of synonymous codons, some of which approximate the codon bias ratio in the overall human proteome; (2) The second class (Class II) disregards the codon bias ratio, and appears to have originated by simple repetition of the same codon (or just a few codons); and finally, (3) In all AARs (including Class I, Class II, and the in-betweens), the codons are chosen in a manner that precludes the formation of RNA secondary structure. It appears that the AAR genes have evolved by orchestrating a balance between codon usage and mRNA secondary structure. The insights gained here should provide a better understanding of AAR evolution and may assist in designing synthetic genes.
first_indexed 2024-04-12T03:08:51Z
format Article
id doaj.art-793ffc34d8b64ebcac9268ab12558eed
institution Directory Open Access Journal
issn 2405-8440
language English
last_indexed 2024-04-12T03:08:51Z
publishDate 2017-12-01
publisher Elsevier
record_format Article
series Heliyon
spelling doaj.art-793ffc34d8b64ebcac9268ab12558eed2022-12-22T03:50:25ZengElsevierHeliyon2405-84402017-12-0131210.1016/j.heliyon.2017.e00492Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon biasSailen BarikA significant number of proteins in all living species contains amino acid repeats (AARs) of various lengths and compositions, many of which play important roles in protein structure and function. Here, I have surveyed select homopolymeric single [(A)n] and double [(AB)n] AARs in the human proteome. A close examination of their codon pattern and analysis of RNA structure propensity led to the following set of empirical rules: (1) One class of amino acid repeats (Class I) uses a mixture of synonymous codons, some of which approximate the codon bias ratio in the overall human proteome; (2) The second class (Class II) disregards the codon bias ratio, and appears to have originated by simple repetition of the same codon (or just a few codons); and finally, (3) In all AARs (including Class I, Class II, and the in-betweens), the codons are chosen in a manner that precludes the formation of RNA secondary structure. It appears that the AAR genes have evolved by orchestrating a balance between codon usage and mRNA secondary structure. The insights gained here should provide a better understanding of AAR evolution and may assist in designing synthetic genes.http://www.sciencedirect.com/science/article/pii/S240584401733548XGeneticsComputational biologyStructural biologyBioinformatics
spellingShingle Sailen Barik
Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon bias
Heliyon
Genetics
Computational biology
Structural biology
Bioinformatics
title Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon bias
title_full Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon bias
title_fullStr Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon bias
title_full_unstemmed Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon bias
title_short Amino acid repeats avert mRNA folding through conservative substitutions and synonymous codons, regardless of codon bias
title_sort amino acid repeats avert mrna folding through conservative substitutions and synonymous codons regardless of codon bias
topic Genetics
Computational biology
Structural biology
Bioinformatics
url http://www.sciencedirect.com/science/article/pii/S240584401733548X
work_keys_str_mv AT sailenbarik aminoacidrepeatsavertmrnafoldingthroughconservativesubstitutionsandsynonymouscodonsregardlessofcodonbias