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. Author manuscript; available in PMC: 2010 Mar 11.
Published in final edited form as: Structure. 2009 Mar 11;17(3):363–373. doi: 10.1016/j.str.2009.01.006

Figure 1.

Figure 1

Heterogeneity in Taf2p content in TFIID purified by different methods.

(A) Sypro Ruby stained SDS-PAGE gel showing the subunit content of either HA-tagged Taf1p (HA) or TAP-tagged Taf1p (two independent preparations, TAP-A and TAP-B) purified TFIID. MW standards were run in parallel (MW) and the TFIID subunits are labeled. The stained gel was scanned (BioRad FX imager) and Taf1p and Taf2p content determined using QuantityOne software (BioRad). (B) Apparent dissociation of a portion of Taf2p from the TFIID holocomplex during Mono-S FPLC chromatography. CaM-Sepharose eluted TAP-TFIID was subjected to Mono-S FPLC chromatography and eluted with 1M NaCl as shown. The protein composition of the fractionated TFIID was measured by SDS-PAGE as in panel A; Fraction number, Molecular weight standards (MW), Input to Mono-S column (In) and unbound proteins (BT) indicated. The Taf2p and Taf1p subunits in the Mono-S 1M salt-eluted fractions are indicated by asterisks.