Key result
TbCof adopts a conserved ADF/cofilin fold to bind G-actin and depolymerize F-actin independently of pH.
Why the study?
The structural and functional characteristics of ADF/cofilin from Trypanosoma brucei were not previously determined.
The study determines the solution structure of ADF/cofilin from Trypanosoma brucei, demonstrating its structural and functional conservation as an actin-binding protein.
No immediate cardiovascular implications; leaves open extension of ADF/cofilin structural insights to parasitic models.
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 β-sheet composed of six β-strands surrounded by five α-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.
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Dai et al. (2013) studied Trypanosoma brucei (basic science). TbCof (ADF/Cofilin from Trypanosoma brucei) was evaluated on Solution structure and actin-binding properties. TbCof adopts a conserved ADF/cofilin fold, binds to G-actin with submicromolar affinity, and depolymerizes F-actin in a pH-independent manner.
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