International Journal of Molecular Zoology 2024, Vol.14, No.3, 166-181 http://animalscipublisher.com/index.php/ijmz 168 Figure 1 PER2 interacts with nuclear receptors (Adopted from Schmutz et al., 2010) Image caption: (A): Structural organization of mouse PER proteins. Gray boxes represent the PAS A, PAS B, and PAC domains. Corepressor-like (CoRNR, yellow) and coactivator like (LXXLL, pink) protein-protein interaction motifs are highlighted. Alignment of the LXXLL sequences of PER1 (blue) and PER2 (red) is shown. Numbers indicate the amino acid positions in the primary structure. (B) PPARa was immunoprecipitated from mouse liver nuclear extracts. Extracts derived from Per2Brdm1 mice were used to monitor the specificity of the antibody against PER2. (C) BMAL1 was immunoprecipitated from mouse liver nuclear extracts. (D) HA-tagged nuclear receptors were expressed in NIH 3T3 cells and were immunoprecipitated from nuclear extracts. Expression vectors used for cotransfection are indicated. (E) PER2 was immunoprecipitated from mouse liver nuclear extracts. An extract derived from Rev-Erba/mice demonstrates the specificity of the antibody against REV-ERBa. Immunoprecipitated proteins were detected by Western blot analysis with the indicated antibodies (on the right). The input is shown in the left panels. On the left side of the panels, the positions of marker bands are indicated (relative molecular weight). Reactions with beads and extract alone were used as controls for nonspecific binding. (ZT) Zeitgeber time (Adopted from Schmutz et al., 2010)
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