The Circadian RNA-Binding Protein CHLAMY 1 Represents a Novel Type Heteromer of RNA Recognition Motif and Lysine Homology Domain-Containing Subunits

• DOI: 10.1128/ec.3.3.815-825.2004
• Publication Date: 2004-06-09T17:22:25Z
• Authors: Bin Zhao; Claudia Schneid; Dobromir Iliev; Eva-Maria Schmidt; Volker Wagner; Franziska Wollnik; Maria Mittag
• Keywords: RNA recognition motif; Chlamydomonas reinhardtii

ABSTRACT The RNA-binding protein CHLAMY 1 from Chlamydomonas reinhardtii binds specifically to UG (≥7) repeat sequences situated in the 3′ untranslated regions of several mRNAs. Its binding activity is controlled by circadian clock. biochemical purification and characterization revealed a novel type protein. It includes two different subunits (named C1 C3), whose interaction appears necessary for RNA binding. One them (C3) belongs proteins CELF (CUG-BP-ETR-3-like factors) family thus bears three recognition motif domains. other composed lysine homology domains protein-protein domain (WW). C3 have theoretical molecular masses 45 52 kDa, respectively, are present nearly equal amounts during cycle. At beginning subjective night, both can be found complexes 100 160 kDa. However, day when low, subunit addition high-molecular-mass complex more than 680 These data indicate posttranslational control 1. Notably, shows significant rat CUG-binding 2. Anti-C3 antibodies recognize homologue, which also this vertebrate.