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. 2006 Mar;26(5):1743–1753. doi: 10.1128/MCB.26.5.1743-1753.2006

FIG.1.

FIG.1.

Functional characterization of the C terminus of mCRY1 in nuclear import. (A) Protein sequence alignment of NLSn and NLSc of mCRY1, human CRY1 (hCRY1), and mCRY2 (amino acid numbers are indicated above the sequence; stop codons are represented by a star). For comparison, the bipartite NLS of nucleoplasmin is aligned with NLSc. Conserved basic amino acids in the NLSs are in boldface type and underlined. Amino acid substitutions, as present in HA-CRY1mutNLSc, HA-CRY1mutNLSn, and HA-CRY1mutNLSn+c, are also indicated. (B) Schematic representation of HA-CRY1, HA-CRY1mutNLSc, HA-CRY1mutNLSn, and HA-CRY1mutNLSn+c. Mutations in NLSc and NLSn are indicated by a star. The photolyase-like domain is shown in dark blue, and the C terminus is shown in light blue. (C) Immunofluorescence pictures of COS7 cells transfected with the constructs shown in B. (D) Quantification of the cellular localization of the above-described proteins. Nuclear (N) signal is black, nuclear/cytoplasmic (N/C) signal is gray, and cytoplasmic (C) signal is red. (E) Schematic representation of HA-CRY1ΔCC, HA-CRY1ΔCCmutNLSc, HA-CRY1ΔCCtail, and HA-CRY1Δtail. The tail is indicated in light blue, and the CC domain is shown in yellow. The left and right red bars represent NLSn and NLSc, respectively, and the star is the mutated NLSc. (F) Immunofluorescence pictures of COS7 cells transfected with the constructs shown in E. αHA, anti-HA. (G) Quantification of the cellular localization of the transiently expressed proteins.