• Login
    View Item 
    •   AUW IR
    • Faculty Research
    • Science & Math
    • Current Faculties
    • Ayan Roy
    • Articles
    • 2015
    • View Item
    •   AUW IR
    • Faculty Research
    • Science & Math
    • Current Faculties
    • Ayan Roy
    • Articles
    • 2015
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Molecular characterization influencing metal resistance in the Cupriavidus/Ralstonia genomes

    Thumbnail
    View/Open
    2015 (2).pdf (1.797Mb)
    Date
    2015
    Author
    Roy, Ayan
    Metadata
    Show full item record
    Abstract
    Our environment is stressed with a load of heavy and toxic metals. Microbes, abundant in our environment are found to adapt well to this metal stressed condition. A comparative study among five Cupriavidus/Ralstonia genomes, can offer a better perception of their evolutionary mechanisms to adapt to these conditions. We have studied codon usage among 1051 genes common to all these organisms and identified 15 optimal codons frequently used in highly expressed genes present within 1051 genes. We found, the core genes of Cupriavidus metallidurans CH34 have a different optimal codon choice for Arginine, Glycine and Alanine in comparison to the other four bacteria. We also found that the synonymous codon-usage bias within these 1051 core genes is highly correlated with their gene expression. This supports that translational selection drives synonymous codon usage in the core genes of these genomes. Synonymous Codon usage is highly conserved in the core genes of these five genomes. The only exception among them is Cupriavidus metallidurans CH34. This genome-wide shift in synonymous codon choice in C. metallidurans CH34 may have taken place due to the insertion of new genes in its genomes facilitating them to survive in heavy-metal containing environment and the co-evolution of the other genes in its genome to achieve a balance in gene expression. Structural studies indicated the presence of a longer N-terminal region containing a copper binding domain in the cupC proteins of C. metallidurans CH3 that helps it to attain higher binding efficacy with copper in comparison to its orthologs.
    URI
    repository.auw.edu.bd:8080//handle/123456789/745
    Collections
    • 2015 [3]

    DSpace software copyright © 2002-2022  LYRASIS
    Contact Us | Send Feedback
    Theme by 
    Atmire NV
     

     

    Browse

    All of AUW Institutional RepositoryCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    LoginRegister

    DSpace software copyright © 2002-2022  LYRASIS
    Contact Us | Send Feedback
    Theme by 
    Atmire NV