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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The glyceraldehyde-3-phosphate dehydrogenase binds in vitro to the SH3 domain of Saccharomyces cerevisiae Cdc25p.

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).[1]

References

  1. The glyceraldehyde-3-phosphate dehydrogenase binds in vitro to the SH3 domain of Saccharomyces cerevisiae Cdc25p. Buu, A., Garreau, H., Jacquet, M. C. R. Acad. Sci. III, Sci. Vie (1995) [Pubmed]
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