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Related Experiment Videos

Induced nucleotide specificity in a GTPase.

Shu-ou Shan1, Peter Walter

  • 1Howard Hughes Medical Institute and Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0448, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 29, 2003
PubMed
Summary
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Bacterial protein targeting relies on Ffh and FtsY GTPases. SRP binding transforms FtsY, enhancing its nucleotide specificity and potentially activating its GTPase activity through a novel mechanism.

Area of Science:

  • Molecular biology
  • Cellular biology
  • Biochemistry

Background:

  • Signal-recognition particle (SRP)-dependent protein targeting is crucial for bacterial plasma membrane insertion.
  • Ffh (SRP subunit) and FtsY (SRP receptor) are GTPases that reciprocally activate each other.
  • The precise mechanism of this GTPase activation remains unclear.

Purpose of the Study:

  • To elucidate the molecular mechanism of reciprocal GTPase activation between Ffh and FtsY.
  • To investigate the nucleotide-binding properties of FtsY in its free and complexed states.
  • To understand how SRP binding influences FtsY's nucleotide specificity.

Main Methods:

  • Comparative analysis of FtsY nucleotide preference in free and complexed states.
  • Investigation of conformational changes in FtsY upon SRP interaction.

Related Experiment Videos

  • Biochemical assays to assess GTPase activity and nucleotide discrimination.

    • Main Results:

    • Free FtsY displays low specificity for GTP over other nucleotides.
    • Formation of the SRP.FtsY complex increases FtsY's nucleotide specificity by 1000-fold.
    • SRP binding induces a conformational switch in FtsY from an 'open' to a 'closed' state, enhancing nucleotide discrimination.

    Conclusions:

    • SRP binding induces significant conformational changes in FtsY, directly impacting its GTP-binding site.
    • The 'closed' state of FtsY enhances discrimination between cognate and non-cognate nucleotides.
    • This conformational change likely contributes to FtsY's GTPase activity activation via a novel mechanism, improving targeting accuracy.