Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Yeast gene TRP5: structure, function, regulation.

H Zalkin, C Yanofsky

    The Journal of Biological Chemistry
    |February 10, 1982
    PubMed
    Summary
    This summary is machine-generated.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    A novel approach to speed up peptide sequencing via MS/MS spectra analysis.

    Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual Conference·2007
    Same author

    Surface analysis of peptide mass spectra to improve time and mass localization.

    Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual Conference·2007
    Same author

    New insights into regulation of the tryptophan biosynthetic operon in Gram-positive bacteria.

    Trends in genetics : TIG·2005
    Same author

    Inhibition of the B. subtilis regulatory protein TRAP by the TRAP-inhibitory protein, AT.

    Science (New York, N.Y.)·2001
    Same author

    The mechanism of tryptophan induction of tryptophanase operon expression: tryptophan inhibits release factor-mediated cleavage of TnaC-peptidyl-tRNA(Pro).

    Proceedings of the National Academy of Sciences of the United States of America·2001
    Same author

    Advancing our knowledge in biochemistry, genetics, and microbiology through studies on tryptophan metabolism.

    Annual review of biochemistry·2001

    Researchers sequenced the yeast TRP5 gene, revealing a bifunctional tryptophan synthase. This enzyme fuses alpha and beta subunits in a reversed order compared to bacteria, with conserved active sites and regulated expression.

    Area of Science:

    • Molecular Biology
    • Yeast Genetics
    • Enzymology

    Background:

    • Tryptophan synthase is a key enzyme in tryptophan biosynthesis.
    • In prokaryotes, tryptophan synthase is typically composed of separate alpha and beta subunits.
    • The genetic organization of tryptophan biosynthesis genes varies across organisms.

    Purpose of the Study:

    • To determine the nucleotide sequence of the yeast TRP5 gene and its flanking regions.
    • To elucidate the structure and evolutionary relationship of yeast tryptophan synthase.
    • To investigate the transcriptional regulation of the TRP5 gene.

    Main Methods:

    • DNA sequencing of the TRP5 gene and flanking regions.
    • Sequence analysis to deduce protein structure and homology.

    Related Experiment Videos

  • S1 nuclease mapping to identify mRNA transcripts.
  • DNA/DNA and RNA/DNA hybridization for gene copy number and expression analysis.

    • Main Results:

    • The yeast TRP5 gene encodes a 2,127 base pair sequence for tryptophan synthase.
    • Yeast tryptophan synthase is a bifunctional protein, a fusion of alpha and beta subunits, with a reversed subunit order compared to E. coli.
    • Conserved active site residues and functionally important amino acids from both E. coli subunits are present in the yeast enzyme.
    • Three major mRNA transcripts with distinct 5' termini were identified.
    • TRP5 gene copy number is elevated in the yeast genome.
    • TRP5 mRNA levels increase significantly upon tryptophan or histidine starvation, indicating transcriptional control.

    Conclusions:

    • Yeast tryptophan synthase possesses a unique fused structure with reversed subunit orientation relative to prokaryotes.
    • Key functional and structural elements of bacterial tryptophan synthase are conserved in the yeast enzyme.
    • The TRP5 gene is transcriptionally regulated in response to amino acid availability.