My NCBISign In

Display Settings:

Format

Send to:

Choose Destination
    Proc Natl Acad Sci U S A. 2009 Feb 24;106(8):2549-53. Epub 2009 Feb 5.

    Thirteen posttranslational modifications convert a 14-residue peptide into the antibiotic thiocillin.

    Wieland Brown LC, Acker MG, Clardy J, Walsh CT, Fischbach MA.

    Source

    Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA.

    Abstract

    The thiazolylpeptides are a family of >50 bactericidal antibiotics that block the initial steps of bacterial protein synthesis. Here, we report a biosynthetic gene cluster for thiocillin and establish that it, and by extension the whole class, is ribosomally synthesized. Remarkably, the C-terminal 14 residues of a 52-residue peptide precursor undergo 13 posttranslational modifications to give rise to thiocillin, making this antibiotic the most heavily posttranslationally-modified peptide known to date.

    PMID:
    19196969
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2650375
    Free PMC Article

    Images from this publication.See all images (4) Free text

    Fig. 2.
    Fig. 4.
    Fig. 1.
    Fig. 3.

    Publication Types, MeSH Terms, Substances, Grant Support

    Publication Types

    MeSH Terms

    Substances

    Grant Support

    LinkOut - more resources

    Full Text Sources

    Other Literature Sources

      Supplemental Content

      Icon for HighWire Press Icon for PubMed Central

      Save items

      loading

      Related citations in PubMed

      See reviews... See all...

      Cited by 26 PubMed Central articles

      See all...

      Related information

      • Related Citations
        Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
      • Compound (MeSH Keyword)
        PubChem chemical compound records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.
      • Protein Clusters
        Clusters of related proteins from the Protein Clusters database that cite the current articles. Sources of references in Protein Clusters include the associated Gene and Conserved Domain records as well as NCBI added citations.
      • References for this PMC Article
        Citation referenced in PubMed article. Only valid for PubMed citations that are also in PMC.
      • Substance (MeSH Keyword)
        PubChem chemical substance (submitted) records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.
      • Taxonomy via GenBank
        Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).
      • Domains
        Conserved Domain Database (CDD) records that cite the current articles. Citations are from the CDD source database records (PFAM, SMART).
      • Protein
        Protein translation features of primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.
      • Free in PMC
        Free full text articles in PMC
      • Cited in PMC
        Full-text articles in the PubMed Central Database that cite the current articles.

      Recent activity

      Clear Turn Off Turn On

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      You are here: NCBI > Literature > PubMed
      Write to the Help Desk