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. Author manuscript; available in PMC: 2023 Jul 31.
Published in final edited form as: Mol Biol Rep. 2007 Mar 24;35(2):215–223. doi: 10.1007/s11033-007-9073-7

Fig. 1.

Fig. 1

Design and structure of proteins used in this study. (A) Amino acid alignments of DRE, mCherry, and mCherry short. The identical aa are indicated by asterisks, non-matching aa are indicated by periods. The position of M182 in DRE is indicated by the vertical arrow, and stretches of identical amino acids that represent overlaps in chimeras are indicated by horizontal lines above the sequence. The precise aa composition of chimeras can be derived by switching between aa sequences of two parental proteins at the region of overlap. E.g., the aa sequence for MD1 can be derived by switching from aa sequence of mCherry to that of DRE at MD1/DM1 region of overlap. Similarly, MD2 aa sequence can derived by switching between these two sequences at the MD2 region. Please note that core aa sequences of mCherry and DRE are different at only 25 positions. (B) The strategy for the construction of MD chimeras. Primers 1 and 4 are mCherryPCRf and DsExprRxba, respectively (Table 1). Primer 3, depending on the chimera number, was either MD1/DM1F, MD2F, MD3F, or MD4F. Similarly, depending on the chimera number, primer 4 was either MD1/DM1R, MD2R, MD3R, or MD4R. The DM1 chimera was constructed similarly using primers DsExprFnoATGbam, MD1/DM1R, MD1/DM1F, and mCherry PCRr as primers 1, 2, 3, and 4, respectively (Table 1 )