Binding of FKBP23 to BiP in ER shown by gel filtration chromatography.
FKBP23 was found in mouse endoplasmic reticulum (ER) in 1998. It consists of an N-terminal peptidyl-prolyl cis/trans isomerase (PPIase) domain and a C-terminal domain with Ca2+ binding sites. Previously, we reported that FKBP23 specifically binds to BiP, the main protein of the molecular chaperone Hsp70 in ER lumen, and the binding is interrelated with the Ca2+ concentration. In this work we have found the existence of the complex FKBP23/BiP by separation of an ER extract using gel filtration chromatography (GFC), and that the existence of this complex is Ca2+-interrelated. This result further verified the Ca2+-interrelated binding of these two proteins in vivo.
Chen
Chen
C
Biochemical Section of Key Laboratory of Functional Polymer Materials, Ministry of Education of China, Institute of Polymer Chemistry, Nankai University, 300071 Tianjin, China.
Ma
Hui
H
Wang
Ying
Y
Mi
Huaifeng
H
D000818:Animals; D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002850:Chromatography, Gel / Q000379:methods; D004721:Endoplasmic Reticulum / Q000378:metabolism; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins / Q000302:isolation & purification / Q000378:metabolism*; D051379:Mice; D018832:Molecular Chaperones / Q000302:isolation & purification / Q000378:metabolism*; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D022021:Tacrolimus Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*
D002135:Calcium-Binding Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; C116295:Fkbp7 protein, mouse; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011994:Recombinant Proteins; D022021:Tacrolimus Binding Proteins