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Conformational isomerization in phage Mu transpososome assembly: effects of the transpositional enhancer and of MuB

M Mizuuchi1, K Mizuuchi

  • 1Laboratory of Molecular Biology, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

The EMBO Journal
|December 1, 2001
PubMed

Insights

Phage Mu transpososome assembly is regulated by cofactors. The internal activation sequence (IAS) enhances later steps, while MuB protein stimulates assembly without needing stable DNA binding for this role.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Phage Mu DNA transposition requires Mu transpososomes, complex protein-DNA structures.
  • Assembly involves MuA transposase, Mu DNA ends, and regulatory cofactors like MuB.
  • The internal activation sequence (IAS) is a key regulatory DNA site.

Purpose of the Study:

  • To investigate how assembly cofactors impact the kinetics of Mu transpososome formation.
  • To identify specific reaction steps influenced by the internal activation sequence (IAS) and MuB protein.

Main Methods:

  • Kinetic analysis of transpososome assembly.
  • Investigating the roles of the internal activation sequence (IAS) and MuB protein.

Main Results:

  • The IAS primarily accelerates post-synaptic conformational changes, not initial DNA end pairing.
  • MuB protein stimulates transpososome assembly without requiring stable DNA binding for this function.
  • MuB's stable DNA binding is crucial for directing transposition to distal sites.

Conclusions:

  • The IAS acts as a late-acting enhancer in Mu transpososome assembly.
  • MuB's role in stimulating assembly is distinct from its role in target site selection.
  • Understanding these cofactor roles provides insight into the regulation of phage transposition.

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