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. 2012 Jun;61(2):324–332. doi: 10.1016/j.parint.2011.12.004

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© 2012 Elsevier Ireland Ltd.

Open Access under CC BY 3.0 license

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Fig. 1 — Sequence analyses. (A) Multiple amino acid sequence alignment of PoDHFR-TS variant (EU266602), PoDHFR-TS classic (EU266606), PfDHFR-TS (J03028), PvDHFR-TS (EU478859), PmDHFR-TS (AY846633), and PkDHFR-TS (XM002258192). Numbers in brackets indicate percent homology to PoDHFR-TS variant EU266602. Amino acids A16, N51, C59, S108, and I164 in PfDHFR-TS and F57, S58, T61, S117, I173 in PvDHFR-TS are highlighted in bold. Mutations at these positions have been reported to be associated with antifolate resistance. Residues known to be important for TS activity are shown as underlined bold letters. T225, T258, W303, Y476, and N478 — for which the errors were found in the encoded nucleotides during the cloning process — are denoted in italic with bold letters. (*) amino acid positions with identical residue, (:) amino acid positions with conserved substitution amino acid, (.) amino acid positions with semi-conserved substitution amino acid, and (non-marked) amino acid positions with non-conserved substitution amino acid. (B) The results by LC-MS/MS of tryptic digested fragments of 74 (solid line), 35 (dotted line), and 32 (dash line) kDa proteins matched to DHFR-TS of P. ovale. Highlighted amino acids are N-terminal sequences obtained by Edman N-terminal sequencing of 74, 35, and 32 kDa proteins. Asterisk (*) and hash (#) symbols represent sequences of 35 and 32 kDa protein respectively, identified by Edman N-terminal sequencing. The first three amino acids (bold letters) are extra residues generated from cloning of podhfr-ts into Nhe I site of pET17b.

Fig. 1 — Sequence analyses. (A) Multiple amino acid sequence alignment of PoDHFR-TS variant (EU266602), PoDHFR-TS classic (EU266606), PfDHFR-TS (J03028), PvDHFR-TS (EU478859), PmDHFR-TS (AY846633), and PkDHFR-TS (XM002258192). Numbers in brackets indicate percent homology to PoDHFR-TS variant EU266602. Amino acids A16, N51, C59, S108, and I164 in PfDHFR-TS and F57, S58, T61, S117, I173 in PvDHFR-TS are highlighted in bold. Mutations at these positions have been reported to be associated with antifolate resistance. Residues known to be important for TS activity are shown as underlined bold letters. T225, T258, W303, Y476, and N478 — for which the errors were found in the encoded nucleotides during the cloning process — are denoted in italic with bold letters. (*) amino acid positions with identical residue, (:) amino acid positions with conserved substitution amino acid, (.) amino acid positions with semi-conserved substitution amino acid, and (non-marked) amino acid positions with non-conserved substitution amino acid. (B) The results by LC-MS/MS of tryptic digested fragments of 74 (solid line), 35 (dotted line), and 32 (dash line) kDa proteins matched to DHFR-TS of P. ovale. Highlighted amino acids are N-terminal sequences obtained by Edman N-terminal sequencing of 74, 35, and 32 kDa proteins. Asterisk (*) and hash (#) symbols represent sequences of 35 and 32 kDa protein respectively, identified by Edman N-terminal sequencing. The first three amino acids (bold letters) are extra residues generated from cloning of podhfr-ts into Nhe I site of pET17b.