Abstract

Telomere repeat factor (AtTRF) derived from Arabidopsis thaliana contains a myb‐like domain that binds to double‐stranded telomeric DNA. We cloned the myb‐like domain of AtTRF (AtTRFmyb ) into a pET‐15b vector and expressed the protein in Escherichia coli. AtTRFmyb was purified using Ni‐affinity chromatography. DNA‐binding mode has been examined by electrophoretic mobility shift assay (EMSA). Fluorescence‐quenching experiments determined a K d value of 6.62 nM between AtTRFmyb and plant telomeric DNA. Data from nuclear magnetic resonance (NMR) spectroscopy together with TALOS+ program provide the secondary structures of AtTRFmyb , suggesting that AtTRFmyb binds its plant telomere DNA with three α‐helices of a DNA‐binding motif.

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