Bovine PrPC directly interacts with alphaB-crystalline
Guihong Sun1, Mingxiong Guo, Ao Shen
1The Modern Virology Research Centre and State Key Laboratory of Virology, College of Life Sciences, Wuhan University, PR China.
Abstract:
We used a bovine brain cDNA library to perform a yeast two-hybrid assay with bovine mature PrP(C) as bait. The screening result showed that alphaB-crystalline interacted with PrP(C). The interaction was further evaluated both in vivo and in vitro with different methods, such as immunofluorescent colocalization, native polyacrylamide-gel electrophoresis, and IAsys biosensor assays. The results suggested that alphaB-crystalline may have the ability to refold denatured prion proteins, and provided first evidence that alphaB-crystalline is directly associated with prion protein.
More Related Videos
Related Concept Videos
Rab Proteins
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Organization
The primary structure of a protein is its amino acid sequence.
Leaky Scanning
G Protein-coupled Receptors
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...


