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. 2009 Sep 24;15(3):259–270. doi: 10.1007/s12192-009-0139-4

Fig. 1.

Fig. 1

Multiple alignment of newly characterised fragments and deduced amino acid sequence (at the first base of the codon) of the isolated heat shock protein 70 kDa. Dots indicate that residues were identical in reference to the top level sequence from the population of Chalamont (N. rhenorhodanensis), called Nrhe_Chalamont_Hsp70, and dashes stand for gaps. Boxed nucleotides represent non-synonymous substitutions, and substitutions in bold are in first or second position of codons. Nucleotides boxed in Nrhe_Chalamont_Hsp70 sequence represent the F307 and R408 primers used in quantitative PCR to quantify HSP70 mRNA. The nucleotides and amino acids are numbered along the right margin. The HSP70 characteristic motifs are underlined in bold, and the eukaryotic ATP-GTP binding site is in italic in the amino acid sequence