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 (1)H, (13)C, and (15)N chemical shift assignments of these two proteins as determined by heteronuclear NMR experiments (at pH 6.5 and temperature 298 K).
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Shukla VK,Kabra A,Yadav R,Ono S,Kumar D,Arora Adoi
10.1007/s12104-014-9588-5subject
Has Abstractpub_date
2015-10-01 00:00:00pages
261-5issue
2eissn
1874-2718issn
1874-270Xpii
10.1007/s12104-014-9588-5journal_volume
9pub_type
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