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

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 Assign

authors

Shukla VK,Kabra A,Yadav R,Ono S,Kumar D,Arora A

doi

10.1007/s12104-014-9588-5

subject

Has Abstract

pub_date

2015-10-01 00:00:00

pages

261-5

issue

2

eissn

1874-2718

issn

1874-270X

pii

10.1007/s12104-014-9588-5

journal_volume

9

pub_type

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