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Effect of codon message on xylanase thermal activity.
Liu, Liangwei; Wang, Linmin; Zhang, Zhang; Wang, Suya; Chen, Hongge.
Afiliación
  • Liu L; Life Science College, Henan Agricultural University, Zhengzhou 450002, China. LLW321@yahoo.com.cn
J Biol Chem ; 287(32): 27183-8, 2012 Aug 03.
Article en En | MEDLINE | ID: mdl-22707716
Because the genetic codon is known for degeneracy, its effect on enzyme thermal property is seldom investigated. A dataset was constructed for GH10 xylanase coding sequences and optimal temperatures for activity (T(opt)). Codon contents and relative synonymous codon usages were calculated and respectively correlated with the enzyme T(opt) values, which were used to describe the xylanase thermophilic tendencies without dividing them into two thermophilic and mesophilic groups. After analyses of codon content and relative synonymous codon usages were checked by the Bonferroni correction, we found five codons, with three (AUA, AGA, and AGG) correlating positively and two (CGU and AGC) correlating negatively with the T(opt) value. The three positive codons are purine-rich codons, and the two negative codons have A-ends. The two negative codons are pyridine-rich codons, and one has a C-end. Comparable with the codon C- and A-ending features, C- and A-content within mRNA correlated negatively and positively with the T(opt) value, respectively. Thereby, codons have effects on enzyme thermal property. When the issue is analyzed at the residual level, the effect of codon message is lost. The codons relating to enzyme thermal property are selected by thermophilic force at nucleotide level.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Xilosidasas / Codón Idioma: En Revista: J Biol Chem Año: 2012 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Xilosidasas / Codón Idioma: En Revista: J Biol Chem Año: 2012 Tipo del documento: Article País de afiliación: China