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Structural transitions during bacteriophage HK97 head assembly

R L Duda1, J Hempel, H Michel

  • 1Department of Biological Sciences, University of Pittsburgh, PA 15260, USA.

Journal of Molecular Biology
|April 7, 1995
PubMed
Summary
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Bacteriophage HK97

Area of Science:

  • Structural biology
  • Virology
  • Biochemistry

Background:

  • Bacteriophage HK97's head shell is built from a major head protein.
  • This protein undergoes cross-linking to form oligomers in the mature head.
  • Prohead maturation involves specific cleavage and assembly steps.

Purpose of the Study:

  • To investigate the mechanism of protein cross-linking in bacteriophage HK97 head formation.
  • To understand the relationship between shell expansion and protein cross-linking.
  • To identify the specific cross-link formed between subunits.

Main Methods:

  • Analysis of bacteriophage mutants accumulating different prohead types (Prohead I and Prohead II).
  • In vitro cross-linking assays under various conditions.

Related Experiment Videos

  • Agarose gel electrophoresis to monitor shell expansion.
  • SDS-PAGE and mass spectrometry to analyze cross-linked peptides.

    • Main Results:

    • Protein cross-linking occurs in vivo and in vitro, requiring shell expansion.
    • Expansion precedes and triggers cross-linking, catalyzed by shell subunits.
    • A specific cross-link between lysine169 and asparagine356 was identified.

    Conclusions:

    • Shell expansion is the trigger for covalent cross-linking of major head protein subunits in bacteriophage HK97.
    • The cross-linking reaction is likely self-catalyzed by the shell subunits.
    • This process is crucial for the structural integrity of the mature phage head.