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. 2011 Jan 6;108(4):1308–1313. doi: 10.1073/pnas.1017085108

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Fig. 5. — The Lhp1p N- and C-termini increase in protease-resistance upon binding pre-tRNAs or U6 snRNA. (A–D) Lhp1p was incubated with either no RNA or the indicated RNAs, followed by digestion with trypsin (A, C, and D) or chymotrypsin (B). In (C), Lhp1p was incubated with or lacking the anticodon stemloop. After SDS-PAGE, protein fragments were visualized by Coomassie blue staining. (E and F) Major products from the trypsin (E) and chymotrypsin (F) digests were identified using mass spectrometry and N-terminal sequencing. Squares, fragments consisting of the La motif and RRM. Open circles, bands detected in the presence of pre-tRNAs or U6 snRNA. The largest band is full-length Lhp1p, while the shorter fragment contains 15–19 amino acids N-terminal to the La motif but lacks the C terminus (Table S1).

Inline graphic — The Lhp1p N- and C-termini increase in protease-resistance upon binding pre-tRNAs or U6 snRNA. (A–D) Lhp1p was incubated with either no RNA or the indicated RNAs, followed by digestion with trypsin (A, C, and D) or chymotrypsin (B). In (C), Lhp1p was incubated with or lacking the anticodon stemloop. After SDS-PAGE, protein fragments were visualized by Coomassie blue staining. (E and F) Major products from the trypsin (E) and chymotrypsin (F) digests were identified using mass spectrometry and N-terminal sequencing. Squares, fragments consisting of the La motif and RRM. Open circles, bands detected in the presence of pre-tRNAs or U6 snRNA. The largest band is full-length Lhp1p, while the shorter fragment contains 15–19 amino acids N-terminal to the La motif but lacks the C terminus (Table S1).