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Eukaryotic Cell, June 2004, p. 815-825, Vol. 3, No. 3
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.3.815-825.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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

Bin Zhao ,1,{dagger},{ddagger} Claudia Schneid,1,{dagger} Dobromir Iliev,1,{dagger} Eva-Maria Schmidt,1 Volker Wagner,1 Franziska Wollnik,2 and Maria Mittag1*

Institut für Allgemeine Botanik, Friedrich-Schiller-Universität Jena, Am Planetarium 1, 07743 Jena,1 Biologisches Institut, Abteilung Tierphysiologie, Universität Stuttgart, Pfaffenwaldring 57, 70550 Stuttgart, Germany2

Received 21 January 2004/ Accepted 12 April 2004

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

* Corresponding author. Mailing address: Institut für Allgemeine Botanik, Friedrich-Schiller-Universität Jena, Am Planetarium 1, 07743 Jena, Germany. Phone: 49 3641 949 201. Fax: 49 3641 949 202. E-mail: M.Mittag{at}uni-jena.de.

{dagger} B.Z., C.S., and D.I. contributed equally to this work.

{ddagger} Present address: Department of Biochemistry, University of Nebraska, Lincoln.

Eukaryotic Cell, June 2004, p. 815-825, Vol. 3, No. 3
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.3.815-825.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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