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. 2004 Oct 11;167(1):161–170. doi: 10.1083/jcb.200312166

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Copyright © 2004, The Rockefeller University Press

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Figure 1. — SSAT specifically binds to the α9 cytoplasmic domain. (a) Plasmid DNA isolated from positive colonies from α9 yeast two-hybrid library screening were cotransformed into yeast with pAS2-1–containing integrin α2, α4, α5, α9, or β1 cytoplasmic domain cDNA. 72 h after the transformation, yeast growth on YPD (-Ade/-His/-Leu/-Trp/α-X-gal) plate was shown. (b) GST pull-down assays with the α9, α2, α4, and α5 cytoplasmic domains fused to GST and immobilized on Glutathione Sepharose 4B. Wild-type SSAT protein was produced by in vitro transcription and translation (IVTT) in the presence of [³⁵S]methionine. Bound proteins were separated by 15% SDS-PAGE and analyzed by autoradiography. 25% of IVTT products were also analyzed and showed the same amount of input. (c) Wild-type and full-length SSAT, NH₂-terminal deletion SSAT (21–171), COOH-terminal deletion mutants (1–161) and (1–141), and enzymatically inactive (dominant negative [DN]) mutant SSAT (R101A/E152K) proteins were produced by IVTT, pulled down by GST-α9, and analyzed as in b.