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Related Experiment Videos

Nucleotide interactions with membrane-bound transporter associated with antigen processing proteins.

Philip Edward Lapinski1, Gayatri Raghuraman, Malini Raghavan

  • 1Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor 48109-0620, USA.

The Journal of Biological Chemistry
|December 27, 2002
PubMed
Summary

The transporter associated with antigen processing (TAP) complex formation enhances nucleotide binding affinity in the TAP2 subunit. TAP1/TAP2 interactions modulate nucleotide binding, indicating functional interdependence within the complex.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • The transporter associated with antigen processing (TAP) is crucial for adaptive immunity.
  • TAP is composed of TAP1 and TAP2 subunits, each containing a nucleotide-binding domain (NBD).
  • Individual TAP1 and TAP2 NBDs exhibit distinct nucleotide binding properties.

Purpose of the Study:

  • To investigate nucleotide binding properties of TAP1/TAP2 complexes.
  • To determine if nucleotide-binding sites within the TAP complex differ in affinity.
  • To elucidate the role of subunit interactions in modulating nucleotide binding.

Main Methods:

  • Utilized fluorescent protein fusion constructs for subunit separation.
  • Employed photo-cross-linkable nucleotide analogs (8-azido-[gamma-(32)P]ATP and 8-azido-[alpha-(32)P]ADP) for binding assays at 4°C.

Related Experiment Videos

  • Analyzed nucleotide binding in wild-type and mutant TAP complexes deficient in nucleotide binding.

    • Main Results:

    • Individually expressed TAP2 showed lower nucleotide affinity than TAP1.
    • Complex formation significantly enhanced TAP2's nucleotide binding affinity.
    • Evidence suggests two ATP-binding sites with similar affinities in TAP1/TAP2 complexes.
    • TAP1/TAP2 NBD interactions contribute to enhanced TAP2 nucleotide binding.

    Conclusions:

    • TAP complex formation modulates nucleotide binding affinity, particularly enhancing the TAP2 site.
    • Subunit interactions within the TAP complex are critical for optimal nucleotide binding.
    • Functional TAP2 nucleotide-binding site is necessary for TAP1 labeling.