Biased usage of synonymous codons has been elucidated under the perspective of cellular tRNA abundance for quite a long time now. Taking advantage of publicly available gene expression data for Saccharomyces cerevisiae, a systematic analysis of the codon and amino acid usages in two different coding regions corresponding to the regular (helix and strand) as well as the irregular (coil) protein secondary structures, have been performed. Our analyses suggest that apart from tRNA abundance, mRNA folding stability is another major evolutionary force in shaping the codon and amino acid usage differences between the highly and lowly expressed genes in S. cerevisiae genome and surprisingly it depends on the coding regions corresponding to the secondary structures of the encoded proteins. This is obviously a new paradigm in understanding the codon usage in S. cerevisiae. Differential amino acid usage between highly and lowly expressed genes in the regions coding for the irregular protein secondary structure in S. cerevisiae is expounded by the stability of the mRNA folded structure. Irrespective of the protein secondary structural type, the highly expressed genes always tend to encode cheaper amino acids in order to reduce the overall biosynthetic cost of production of the corresponding protein. This study supports the hypothesis that the tRNA abundance is a consequence of and not a reason for the biased usage of amino acid between highly and lowly expressed genes. (c) 2007 Elsevier Inc. All rights reserved.
机构:
Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences
Shandong Energy Institute
Qingdao New Energy Shandong LaboratoryQingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences
Senbiao Fang
Ren Wei
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Junior Research Group Plastic Biodegradation, Institute of Biochemistry, University of GreifswaldQingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences
Ren Wei
Yinglu Cui
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AIMCenter, Institute of Microbiology, Chinese Academy of SciencesQingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences
Yinglu Cui
Lin Su
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Yusuf Hamied Department of Chemistry, University ofQingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences
机构:
KTH Royal Inst Technol, Engn Phys Program, SE-10077 Stockholm, Sweden
AlbaNova Univ Ctr, Dept Computat Biol, S-10691 Stockholm, SwedenKTH Royal Inst Technol, Engn Phys Program, SE-10077 Stockholm, Sweden
Ekeberg, Magnus
Hartonen, Tuomo
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Aalto Univ, Dept Informat & Comp Sci, FI-00076 Aalto, Finland
Univ Helsinki, Biomedicum Helsinki, Masters Degree Programme Translat Med, FI-00014 Helsinki, FinlandKTH Royal Inst Technol, Engn Phys Program, SE-10077 Stockholm, Sweden
Hartonen, Tuomo
Aurell, Erik
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AlbaNova Univ Ctr, Dept Computat Biol, S-10691 Stockholm, Sweden
Aalto Univ, Dept Informat & Comp Sci, FI-00076 Aalto, Finland
Aalto Sci Inst, FI-00076 Aalto, FinlandKTH Royal Inst Technol, Engn Phys Program, SE-10077 Stockholm, Sweden