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Related Experiment Videos

Co-expressed recombinant human Translin-Trax complex binds DNA.

Gagan D Gupta1, Ravindra D Makde, Radhika P Kamdar

  • 1Synchrotron Radiation Section, Bhabha Atomic Research Centre, Mumbai 400 085, India.

FEBS Letters
|May 28, 2005
PubMed
Summary

Translin and Trax proteins form a stable, soluble complex essential for DNA binding. Translin acts as a chaperone, enabling Trax to form functional heteromeric complexes.

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Area of Science:

  • Molecular Biology
  • Protein Biochemistry

Background:

  • Trax protein aggregates into insoluble complexes when expressed alone.
  • Co-expression with Translin protein leads to soluble and stable heteromeric complex formation.

Purpose of the Study:

  • To investigate the complex formation between Trax and Translin proteins.
  • To determine the stoichiometry and DNA-binding properties of the heteromeric complex.

Main Methods:

  • Co-expression of Trax and Translin proteins.
  • Purification of the heteromeric complex.
  • Mass spectrometry (MALDI-TOF-MS) for molecular weight estimation.
  • DNA binding assays (gel shift).

Main Results:

  • Trax and Translin form a stable heteromeric complex (approx. 430 kDa) at nearly equimolar ratios.

Related Experiment Videos

  • Mass spectrometry suggests possible compositions of octameric Translin/hexameric Trax, heptameric Translin/heptameric Trax, or hexameric Translin/octameric Trax.
  • The heteromeric complex binds both single-stranded and double-stranded DNA.

    • Conclusions:

    • Translin protein acts as a chaperone for Trax protein, facilitating the formation of a soluble and DNA-binding competent heteromeric complex.
    • The stoichiometry of the complex is likely octameric Translin with hexameric Trax, or heptameric for both, or hexameric Translin with octameric Trax.
    • The Translin-Trax complex is functionally important for DNA binding.