Related Experiment Video
Updated: Aug 17, 2026

CD Spectroscopy to Study DNA-Protein Interactions
Published on: February 10, 2022
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.
Abstract:
Trax, expressed alone aggregates into insoluble complexes, whereas upon co-expression with Translin becomes readily soluble and forms a stable heteromeric complex ( approximately 430 kDa) containing both proteins at nearly equimolar ratio. Based on the subunit molecular weights, estimated by MALDI-TOF-MS, the purified complex appears to comprise of either an octameric Translin plus a hexameric Trax (calculated MW 420 kDa) or a heptamer each of Trax and Translin (calculated MW 425 kDa) or a hexameric Translin plus an octameric Trax (calculated MW 431 kDa). The complex binds single-stranded/double-stranded DNA. ssDNA gel-shifted complex shows both proteins at nearly equimolar ratio, suggesting that Translin "chaperones" Trax and forms heteromeric complex that is DNA binding competent.
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