Abstract
The actin filament dynamics in nematode, Caenorhabditis elegans, is regulated by differential activity of two proteins UNC-60A and UNC-60B. UNC-60A exhibits strong pointed end depolymerization on C. elegans actin (Ce-actin), strong inhibition of polymerization, strong monomer sequestering activity, weak severing activity, and low affinity for F-actin binding, while UNC-60B exhibits strong pointed end depolymerization on rabbit muscle actin, strong severing activity, and high affinity for F-actin binding. Structural characterization of these proteins will help to understand (1) molecular mechanism of actin dynamics regulation and (2) the differential activity of these proteins. Here, we report 1H, 13C, and 15N chemical shift assignments of these two proteins as determined by heteronuclear NMR experiments (at pH 6.5 and temperature 298 K).
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Acknowledgments
We are thankful to Dr. C.L. Khetrapal for usage of 800 MHz NMR spectrometer at the Centre for Biomedical Research, Lucknow. This work was supported by Council of Scientific and Industrial Research (CSIR) Network Project UNSEEN, and National Biosciences Award Grant from Department of Biotechnology (DBT), to AA. V.K.S. is a recipient of research fellowship from CSIR, New Delhi, India. R.Y. and A.K. are recipients of research fellowship from DBT and Indian Council for Medical Research, New Delhi, India, respectively. Work relating to unc-60a and unc-60b clones was supported by a Grant from National Institutes of Health (AR048615) to S.O.
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Shukla, V.K., Kabra, A., Yadav, R. et al. NMR assignments of actin depolymerizing factor (ADF) like UNC-60A and cofilin like UNC-60B proteins of Caenorhabditis elegans . Biomol NMR Assign 9, 261–265 (2015). https://doi.org/10.1007/s12104-014-9588-5
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DOI: https://doi.org/10.1007/s12104-014-9588-5