Figure S1 - Identification of a Small TAF Complex and Its Role in the Assembly of TAF-Containing Complexes

Pair wise BestFit alignment between the C-terminal half of yeast Spt7p and the whole length human SPT7-Like protein (see O94864 and AAG47636). The amino acid positions in the different sequences are labelled on the left and on the right. The peptides identified in hSPT7L by MALDI TOFF mass spectrometry are shown in bold and with capital letters. When two peptides follow in a row the trypsin-cutting site is shown by a black triangle. The putative histone fold domain (HFD) in both proteins is over layered (according to [1]). Percent similarity between the two proteins is: 45.98% and percent identity is 22.86%. 1) Gangloff YG, Sanders SL, Romier C, Kirschner D, Weil PA, et al. (2001) Histone folds mediate selective heterodimerization of yeast TAF(II)25 with TFIID components yTAF(II)47 and yTAF(II)65 and with SAGA component ySPT7. Mol Cell Biol 21: 1841–1853
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