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De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data
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CONCUR: quick and robust calculation of codon usage from ribosome profiling data.

Michaela Frye1, Susanne Bornelöv2

  • 1Cell Biology and Tumor Biology, German Cancer Research Center (DKFZ), 69120 Heidelberg, Germany.

Bioinformatics (Oxford, England)
|September 1, 2020
PubMed
Summary
This summary is machine-generated.

CONCUR is a new tool for analyzing codon usage in ribosome profiling data. It estimates codon counts at key ribosome positions using aligned sequencing reads.

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Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Genomics

Background:

  • Ribosome profiling is a key technique for studying gene expression at the translational level.
  • Understanding codon usage bias is crucial for deciphering translational regulation and efficiency.
  • Existing tools may not fully capture codon-level dynamics within the ribosome.

Purpose of the Study:

  • To introduce CONCUR, a novel standalone tool for detailed codon usage analysis.
  • To enable precise estimation of codon counts at specific ribosome-protected fragment (RPF) sites.
  • To facilitate the analysis of ribosome dynamics during translation.

Main Methods:

  • CONCUR processes aligned sequencing reads in Binary Alignment Map (BAM) format.
  • The tool quantifies codon counts at the E-, P-, and A-sites of the ribosome.
  • It also analyzes codon counts at positions flanking the A-site.

Main Results:

  • CONCUR provides site-specific codon count estimations from ribosome profiling data.
  • The tool allows for in-depth analysis of codon usage patterns within the translating ribosome.
  • Enables a more granular understanding of translational efficiency and regulation.

Conclusions:

  • CONCUR offers a valuable addition to the bioinformatics toolkit for ribosome profiling analysis.
  • The tool facilitates the investigation of codon-level translational control mechanisms.
  • CONCUR supports research into the intricacies of gene expression and protein synthesis.