GC bias lead to increased small amino acids and random coils of proteins in cold-water fishes ...

Abstract Background Temperature adaptation of biological molecules is fundamental in evolutionary studies but remains unsolved. Fishes living in cold water are adapted to low temperatures through adaptive modification of their biological molecules, which enables their functioning in extreme cold. To...

Full description

Bibliographic Details
Main Authors: Zhang, Dongsheng, Hu, Peng, Liu, Taigang, Wang, Jian, Jiang, Shouwen, Xu, Qianghua, Chen, Liangbiao
Format: Article in Journal/Newspaper
Language:unknown
Published: figshare 2018
Subjects:
Online Access:https://dx.doi.org/10.6084/m9.figshare.c.4088288.v1
https://springernature.figshare.com/collections/GC_bias_lead_to_increased_small_amino_acids_and_random_coils_of_proteins_in_cold-water_fishes/4088288/1
Description
Summary:Abstract Background Temperature adaptation of biological molecules is fundamental in evolutionary studies but remains unsolved. Fishes living in cold water are adapted to low temperatures through adaptive modification of their biological molecules, which enables their functioning in extreme cold. To study nucleotide and amino acid preference in cold-water fishes, we investigated the substitution asymmetry of codons and amino acids in protein-coding DNA sequences between cold-water fishes and tropical fishes., The former includes two Antarctic fishes, Dissostichus mawsoni (Antarctic toothfish), Gymnodraco acuticeps (Antarctic dragonfish), and two temperate fishes, Gadus morhua (Atlantic cod) and Gasterosteus aculeatus (stickleback), and the latter includes three tropical fishes, including Danio rerio (zebrafish), Oreochromis niloticus (Nile tilapia) and Xiphophorus maculatus (Platyfish). Results Cold-water fishes showed preference for Guanines and cytosines (GCs) in both synonymous and nonsynonymous codon ...