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Related Experiment Videos

Still looking for the Ivory Tower.

H K Schachman1

  • 1Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720-3206, USA. schach@socrates.berkeley.edu

Annual Review of Biochemistry
|August 31, 2000
PubMed
Summary

This research details the discovery of ribosomes and chromatophores, and the development of ultracentrifuge techniques. Studies on aspartate transcarbamoylase revealed distinct subunits and conformational changes, advancing our understanding of enzyme regulation and allostery.

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In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.

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Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: implications for allosteric regulation.

Proceedings of the National Academy of Sciences of the United States of America·2000

Area of Science:

  • Biochemistry and Molecular Biology
  • Biophysical Chemistry
  • Enzyme Kinetics and Regulation

Background:

  • Pioneering research utilizing ultracentrifugation techniques to study biological macromolecules.
  • Discovery of novel cellular components including ribonucleoprotein complexes (ribosomes) and chromatophores.
  • Development of advanced ultracentrifuge optical systems (photoelectric absorption and Rayleigh interferometer).

Discussion:

  • Investigated the structure and function of Escherichia coli aspartate transcarbamoylase (ATCase).
  • Elucidated the presence of distinct catalytic and regulatory subunits within ATCase.
  • Characterized global conformational changes in ATCase related to allosteric regulation.

Key Insights:

  • Demonstrated shared active sites in ATCase through mutant hybrids, indicating cooperative subunit interactions.

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  • Established ATCase as a model system for understanding allosteric regulation.
  • Identified distinct roles for catalytic and regulatory subunits in enzyme function.

    • Outlook:

    • Continued investigation of ATCase using protein chemistry and molecular biology techniques.
    • Exploration of enzyme assembly pathways and subunit interactions.
    • Leveraging new crystal structure data to probe ATCase activation mechanisms and allosteric transitions.