title: The glyceraldehyde-3-phosphate dehydrogenase binds in vitro to the SH3 domain of Saccharomyces cerevisiae Cdc25p.
abstract: In order to isolate yeast proteins able to bind to the SH3 domain of the Cdc25p exchange factor, a biochemical approach was used. The SH3 (src homolog type 3) domain of yeast Cdc25p, fused both to a tail of 6 histidine (His) and to glutathione-S-transferase (GST), was purified and then, using His affinity for Ni2+ ions, bound to a Ni-NTA column. This column was used for isolating yeast proteins which have affinity for the yeast SH3-Cdc25p domain. The major protein thus isolated, was sequenced and identified as a yeast glyceraldehyde-3-phosphate dehydrogenase (GAP3DH).
authors.affiliation: Institut de génétique et microbiologie, CNRS URA D1354, Université Paris-XI, Orsay, France.
authors.forename: A
authors.initials: A
authors.lastname: Buu
authors.forename: H
authors.initials: H
authors.lastname: Garreau
authors.forename: M
authors.initials: M
authors.lastname: Jacquet
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D001426:Bacterial Proteins / Q000302:isolation & purification; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification / Q000378:metabolism*; D066298:In Vitro Techniques; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000737:chemistry*; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000201:enzymology; D020666:ras-GRF1
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D010446:Peptide Fragments; D020666:ras-GRF1; C068142:glyceraldehyde 3-phosphate dehydrogenase (304-313); D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010749:Phosphoprotein Phosphatases