Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations.

Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. Abstract Text:

    s d emrS D Emr,p j bassfordP J Bassford,

    Mutations at three genetic loci (termed prlA,B,C) were previously shown to specifically suppress signal sequence mutations in the lamB gene encoding the outer membrane phage lambda receptor protein of Escherichia coli (Emr, S. D., Hanley-Way, S., and Silhavy, T. J. (1981) Cell 23, 79-88). The majority of these suppressor mutations map at the prlA locus and are thought to result in an altered ribosomal protein. In this study, we demonstrate that prlA mutations also phenotypically suppress signal sequence mutations in the malE gene encoding the periplasmic maltose-binding protein. For both lamB and malE mutations, suppression is achieved by transporting the export-defective protein to its correct extracytoplasmic location, in some instances with near 100% efficiency. With a single exception, the mutant-exported protein is apparently processed to its normal mature form. These results indicate that prlA-mediated protein export occurs via the usual route, and additional data suggest that the prlA product directly interacts with the mutant signal sequence to restore export. The single prlC allele also suppresses malE signal sequence mutations, whereas the single prlB allele only phenotypically suppresses lamB signal sequence mutations. However, with these latter two suppressors, there is some indication that export of the phage lambda receptor to the outer membrane is not accomplished by the usual route.

    Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. Publishing Authors By Initials

    sd emrSD Emr,pj bassfordPJ Bassford,

    For similar genetic processes: mutagenesis: suppression, genetic research abstracts see: genetic processes: mutagenesis: suppression, genetic research

    PUBMED ID PMID:

    MEDLINE DATE:

    Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: The Journal of biological chemistry

    VOLUME: 257

    Page Numbers: 5852-60

    Journal Abbreviation: J. Biol. Chem.

    ISSN: 0021-9258

    DAY: 25

    MONTH: May

    YEAR: 1982

    Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 2985121

    Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. Keywords Mesh Terms:

    KEYWORDS: Suppression, Genetic

    MESH TERMS: genetics

    Chemical & Substance for Abstract: Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations. Information

    Substance Name: maltoporins

    Registry Number: 0

    Grant and Affiliation Information for Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations.

    AFFILIATION:

    Country: UNITED STATES

    UNITED STATES Research PublicationUNITED STATES Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: J Biol Chem

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News