Article
In vivo analysis of the lumenal binding protein (BiP) reveals multiple functions of its ATPase domain.
The Plant journal : for cell and molecular biology - 1 Dec 2007
Snowden Christopher James, Leborgne-Castel Nathalie, Wootton Lucie Jan, Hadlington Jane Louise, Denecke Jurgen
Abstract excerpt
The endoplasmic reticulum (ER) chaperone binding protein (BiP) binds exposed hydrophobic regions of misfolded proteins. Cycles of ATP hydrolysis and nucleotide exchange on the ATPase domain were shown to regulate the function of the ligand-binding domain in vitro. Here we show that ATPase mutants of BiP with defective ATP-hydrolysis (T46G) or ATP-binding (G235D) caused permanent association with a model ligand,...
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