Complete amino acid sequence of puroindoline, a new basic and cystine-rich protein with a unique tryptophan-rich domain, isolated from wheat endosperm by Triton X-114 phase partitioning.
A new basic protein has been isolated from wheat endosperm by Triton X-114 phase partitioning. It contains five disulfide bridges and is composed of equal amounts of a polypeptide chain of 115 amino acid residues and of the same chain with a C-terminus dipeptide extension. The most striking sequence feature is the presence of a unique tryptophan-rich domain so that this protein isolated from wheat seeds has been named puroindoline. The similar phase partitioning behavior in Triton X-114 of this basic cystine-rich protein and of purothionins suggests that puroindoline may also be a membranotoxin that might play a role in the defense mechanism of plants against microbial pathogens.
Blochet
J E
JE
Laboratoire de Biochimie et Technologie des Protéines, INRA, Nantes, France.
Chevalier
C
C
Forest
E
E
Pebay-Peyroula
E
E
Gautier
M F
MF
Joudrier
P
P
Pézolet
M
M
Marion
D
D
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D003553:Cystine / Q000032:analysis; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D017830:Octoxynol; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D011092:Polyethylene Glycols; D016415:Sequence Alignment; D014908:Triticum / Q000737:chemistry*; D014364:Tryptophan / Q000032:analysis
D003902:Detergents; D010940:Plant Proteins; C082942:puroindoline protein, Triticum aestivum; D011092:Polyethylene Glycols; D003553:Cystine; D014364:Tryptophan; D017830:Octoxynol; C010615:Nonidet P-40