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Related Experiment Videos

Nucleotide binding by the synapse associated protein SAP90

U Kistner1, C C Garner, M Linial

  • 1Department of Biological Chemistry, Hebrew University, Jerusalem, Israel.

FEBS Letters
|February 13, 1995
PubMed
Summary

The synapse associated protein SAP90 specifically binds GMP, a guanine nucleotide, but shows no guanylate kinase activity. This finding highlights the importance of GMP binding in the evolution of related cell-contact proteins.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Synapse associated protein SAP90 (SAP90) is found at cell-cell contact sites.
  • SAP90 belongs to a protein superfamily with guanylate kinase-like domains, including SAP97, dlg-Ap, ZO-1, ZO-2, and p55.

Purpose of the Study:

  • To investigate the nucleotide binding properties of SAP90.
  • To determine if SAP90 possesses guanylate kinase activity.

Main Methods:

  • The study focused on analyzing the specific binding affinities of SAP90 to various guanine and adenine nucleotides.
  • Experimental conditions were established to detect potential guanylate kinase activity.

Main Results:

  • SAP90 demonstrated specific binding to GMP within the micromolar range.

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  • Binding to ATP, GDP, and ADP was observed at significantly lower affinities (10-25 mM).
  • No guanylate kinase activity was detected for SAP90 under the tested conditions.

    • Conclusions:

    • The specific GMP binding capacity of SAP90 is a significant characteristic.
    • The conservation of the guanylate kinase domain within this superfamily may serve an evolutionary role related to GMP binding.