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- Title
Structural and Functional Insight into ADF/Cofilin from Trypanosoma brucei.
- Authors
Kun Dai; Shanhui Liao; Jiahai Zhang; Xuecheng Zhang; Xiaoming Tu; Kursula, Inari
- Abstract
The ADF/cofilin family has been characterized as a group of actin-binding proteins critical for controlling the assembly of actin within the cells. In this study, the solution structure of the ADF/cofilin from Trypanosoma brucei (TbCof) was determined by NMR spectroscopy. TbCof adopts the conserved ADF/cofilin fold with a central b-sheet composed of six b- strands surrounded by five a-helices. Isothermal titration calorimetry experiments denoted a submicromolar affinity between TbCof and G-actin, and the affinity between TbCof and ADP-G-actin was five times higher than that between TbCof and ATP-G-actin at low ionic strength. The results obtained from electron microscopy and actin filament sedimentation assays showed that TbCof depolymerized but did not co-sediment with actin filaments and its ability of F- actin depolymerization was pH independent. Similar to actin, TbCof was distributed throughout the cytoplasm. All our data indicate a structurally and functionally conserved ADF/cofilin from Trypanosoma brucei.
- Subjects
ACTIN research; CELLS; SPECTRUM analysis; CALORIMETRY; ELECTRON microscopes; CYTOPLASM; TRYPANOSOMA brucei
- Publication
PLoS ONE, 2013, Vol 8, Issue 1, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0053639