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. 1998 Jul 21;95(15):8538–8543. doi: 10.1073/pnas.95.15.8538

Figure 4.

Figure 4

Sequence alignments. (A) Mouse and C. elegans Rgr1 homologs. Sequence analysis of the p110 component of mouse Mediator yielded two peptides (underlined) matching the sequence expected from mouse EST AA562494 translated in the +2 frame. The DNA sequence of EST AA562494 partially overlapped that of EST AA204093, and fusion of the two DNA sequences and translation generated the 233-residue mouse sequence shown. A blast search with this sequence revealed the homology with C. elegans Rgr1 shown. A third peptide from p110 was mapped to a region of the 233-residue mouse sequence (indicated by asterisks) on the basis of its experimental mass (m/z = 2122.097), which was in excellent agreement with the calculated monoisotopic mass of the expected peptide [(MH+) = 2122.123, Δ = 0.026 Da (12 ppm)]. (B) Yeast Rgr1 and C. elegans Rgr1 homolog. (C) Human homolog of the p28a component of mouse Mediator and Drosophila Trf-proximal. Peptide sequences obtained from p28a are underlined. A difference between human and mouse sequences is indicated by an asterisk.