4.3 Article

A draft genome assembly for the eastern fox squirrel, Sciurus niger

Journal

G3-GENES GENOMES GENETICS
Volume 11, Issue 12, Pages -

Publisher

OXFORD UNIV PRESS INC
DOI: 10.1093/g3journal/jkab315

Keywords

whole-genome sequencing; de novo assembly; tree squirrels; candidate genes; heme biosynthesis; color vision; hibernation; eastern fox squirrel; Sciurus niger; Sciuridae

Funding

  1. Virginia Museum of Natural History Foundation

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The study assembled a draft genome of the eastern fox squirrel, predicted a large number of protein-encoding genes, annotated repeat elements, and showed consistency in the species tree topology. The genome assembly can be valuable for studies of genome structure and function, population genomics, and biomedical research.
The eastern fox squirrel, Sciurus niger, exhibits marked geographic variation in size and coat color, is a model organism for studies of behavior and ecology, and a potential model for investigating physiological solutions to human porphyrias. We assembled a genome using Illumina HiSeq, PacBio SMRT, and Oxford Nanopore MinION sequencing platforms. Together, the sequencing data resulted in a draft genome of 2.99 Gb, containing 32,830 scaffolds with an average size of 90.9 Kb and N 50 of 183.8 Kb. Genome completeness was estimated to be 93.78%. A total of 24,443 protein-encoding genes were predicted from the assembly and 23,079 (94.42%) were annotated. Repeat elements comprised an estimated 38.49% of the genome, with the majority being LINEs (13.92%), SINEs (6.04%), and LTR elements. The topology of the species tree reconstructed using maximum-likelihood phylogenetic analysis was congruent with those of previous studies. This genome assembly can prove useful for comparative studies of genome structure and function in this rapidly diversifying lineage of mammals, for studies of population genomics and adaptation, and for biomedical research. Predicted amino acid sequence alignments for genes affecting heme biosynthesis, color vision, and hibernation showed point mutations and indels that may affect protein function and ecological adaptation.

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