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Effect of codon message on xylanase thermal activity.

Liangwei Liu1, Linmin Wang, Zhang Zhang

  • 1Life Science College, Henan Agricultural University, Zhengzhou 450002, China. LLW321@yahoo.com.cn

The Journal of Biological Chemistry
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Genetic codons influence enzyme thermal properties. Specific codon patterns in GH10 xylanase genes correlate with optimal activity temperatures, revealing nucleotide-level selection for thermophilic tendencies.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzyme kinetics

Background:

  • Enzyme thermal properties are crucial for industrial applications.
  • The influence of genetic codon degeneracy on enzyme thermotolerance is largely unexplored.
  • GH10 xylanases are important industrial enzymes with varying optimal temperatures.

Purpose of the Study:

  • To investigate the correlation between codon usage and the optimal temperature (T(opt)) of GH10 xylanases.
  • To identify specific codons associated with thermophilic tendencies in enzymes.
  • To understand the role of nucleotide composition in enzyme thermal adaptation.

Main Methods:

  • Construction of a dataset of GH10 xylanase coding sequences and their T(opt) values.
  • Calculation of codon content and relative synonymous codon usage (RSCU).
  • Statistical correlation analysis between codon metrics and T(opt), including Bonferroni correction.

Main Results:

  • Five codons (AUA, AGA, AGG, CGU, AGC) showed significant correlation with T(opt).
  • Purine-rich, A-ending codons (AUA, AGA, AGG) positively correlated with T(opt).
  • Pyridine-rich, C/A-ending codons (CGU, AGC) negatively correlated with T(opt).
  • mRNA C- and A-content correlated negatively and positively with T(opt), respectively.

Conclusions:

  • Genetic codons significantly impact enzyme thermal properties, specifically T(opt).
  • Codon selection at the nucleotide level contributes to enzyme thermophilic adaptation.
  • The effect of codon bias on thermal properties is lost when analyzed at the amino acid (residual) level.