Characterization of the dystrophin-syntrophin interaction using the two-hybrid system in yeast.
The carboxy-terminal region of dystrophin has previously been shown to interact directly with alpha1 syntrophin, a cytoplasmic component of the dystrophin-glycoprotein complex, by in vitro biochemical studies such as overlay assay or immunoprecipitation. Using the two-hybrid system, we have isolated from a human heart cDNA library the entire coding sequence of human alpha1 syntrophin, therefore confirming for the first time this interaction via an in vivo approach. In addition, we have reduced the interaction domain to the distal half of alpha1 syntrophin.
Castelló
A
A
U. 129 INSERM, Institut Cochin de Génétique Moléculaire, Paris, France.
Brochériou
V
V
Chafey
P
P
Kahn
A
A
Gilgenkrantz
H
H
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D002135:Calcium-Binding Proteins; D003001:Cloning, Molecular; D017124:Conserved Sequence; D017931:DNA Primers; D016189:Dystrophin / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009206:Myocardium / Q000737:chemistry; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000235:genetics; D016415:Sequence Alignment; D017421:Sequence Analysis; D014170:Transformation, Genetic / Q000235:genetics
D002135:Calcium-Binding Proteins; D017931:DNA Primers; D016189:Dystrophin; D008565:Membrane Proteins; D009124:Muscle Proteins; C091825:syntrophin alpha1