• Login
    View Item 
    •   Maryland Shared Open Access Repository Home
    • ScholarWorks@UMBC
    • UMBC College of Natural and Mathematical Sciences
    • UMBC Biological Sciences Department
    • View Item
    •   Maryland Shared Open Access Repository Home
    • ScholarWorks@UMBC
    • UMBC College of Natural and Mathematical Sciences
    • UMBC Biological Sciences Department
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Altered regulation of the glnRA operon in a Bacillus subtilis mutant that produces methionine sulfoximine-tolerant glutamine synthetase

    Thumbnail
    Links to Files
    https://www.ncbi.nlm.nih.gov/pubmed/8093698
    Permanent Link
    https://doi.org/10.1128/jb.175.3.892-897.1993
    http://hdl.handle.net/11603/13075
    Collections
    • UMBC Biological Sciences Department
    • UMBC Department of Marine Biotechnology
    • UMBC Faculty Collection
    Metadata
    Show full item record
    Author/Creator
    H. J., Schreier
    C. A., Rostkowski
    E. M., Kellner
    Date
    1993-02
    Type of Work
    6 pages
    Text
    journal articles
    Citation of Original Publication
    H J Schreier, C A Rostkowski, E M Kelln, Altered regulation of the glnRA operon in a Bacillus subtilis mutant that produces methionine sulfoximine-tolerant glutamine synthetase, J Bacteriol. 1993 Feb;175(3):892-7, DOI: 10.1128/jb.175.3.892-897.1993
    Rights
    This item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
    Subjects
    Bacillus subfilis
    glutamine synthetase (GS)
    DL-methionine sulfoximine
    Lmethionine-SR-sulfoximine (MSX)
    Abstract
    A Bacillus subfilis mutant that produced glutamine synthetase (GS) with altered sensitivity to DL-methionine sulfoximine was isolated. The mutation, designated glnA33, was due to a T- A-to-C- G transition, changing valine to alanine at codon 190 within the active-site C domain. Altered regulation was observed for GS activity and antigen and mRNA levels in a B. subtilis glnA33 strain. The mutant enzyme was 28-fold less sensitive to DL-methionine sulfoximine and had a 13.0-fold-higher Km for hydroxylamine and a 4.8-fold-higher Km for glutamate than wild-type GS did.


    Albin O. Kuhn Library & Gallery
    University of Maryland, Baltimore County
    1000 Hilltop Circle
    Baltimore, MD 21250
    www.umbc.edu/scholarworks

    Contact information:
    Email: scholarworks-group@umbc.edu
    Phone: 410-455-3021


    If you wish to submit a copyright complaint or withdrawal request, please email mdsoar-help@umd.edu.

     

     

    My Account

    LoginRegister

    Browse

    This CollectionBy Issue DateTitlesAuthorsSubjectsType

    Statistics

    View Usage Statistics


    Albin O. Kuhn Library & Gallery
    University of Maryland, Baltimore County
    1000 Hilltop Circle
    Baltimore, MD 21250
    www.umbc.edu/scholarworks

    Contact information:
    Email: scholarworks-group@umbc.edu
    Phone: 410-455-3021


    If you wish to submit a copyright complaint or withdrawal request, please email mdsoar-help@umd.edu.