Proteomic approaches to identify cold-regulated plasma membrane proteins.
Plasma membrane is the primary determinant of freezing tolerance in plants because of its central role in freeze-thaw cycle. Changes in the plasma membrane proteins have been one of the major research areas in plant cold acclimation. To obtain comprehensive profiles of the plasma membrane proteomes and their changes during the cold acclimation process, a plasma membrane purification method using a dextran-polyethylene glycol two polymer system and a mass spectrometry-based shotgun proteomics method using nano-LC-MS/MS for the plasma membrane proteins are described. The proteomic results obtained are further applied to label-free protein semiquantification.
United Graduate School of Agricultural Sciences, Iwate University, 3-18-8 Ueda, Morioka, Iwate, 020-8550, Japan.
Daisuke
D
Takahashi
Takato
T
Nakayama
Yushi
Y
Miki
Yukio
Y
Kawamura
Matsuo
M
Uemura
D000064:Acclimatization; D017360:Arabidopsis / Q000166:cytology / Q000378:metabolism / Q000502:physiology; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002853:Chromatography, Liquid; D003080:Cold Temperature; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D036103:Nanotechnology; D020543:Proteome / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D053719:Tandem Mass Spectrometry; D014357:Trypsin / Q000378:metabolism
D029681:Arabidopsis Proteins; D008565:Membrane Proteins; D020543:Proteome; D014357:Trypsin