NMR assignments of actin depolymerizing factor (ADF) like UNC-60A and cofilin like UNC-60B proteins of Caenorhabditis elegans

作者：Shukla Vaibhav Kumar; Kabra Ashish; Yadav Rahul; Ono Shoichiro; Kumar Dinesh; Arora Ashish^*

来源：Biomolecular NMR Assignments, 2015, 9(2): 261-265.

DOI：10.1007/s12104-014-9588-5

• NMR
• Resonance assignment
• ADF like protein
• UNC-60A
• UNC-60B

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 H-1, C-13, and N-15 chemical shift assignments of these two proteins as determined by heteronuclear NMR experiments (at pH 6.5 and temperature 298 K).

• 出版日期2015-10