Novel interaction of two clock-relevant RNA-binding proteins C3 and XRN1 in Chlamydomonas reinhardtii

• Published in: FEBS letters Vol. 586; no. 22; pp. 3969 - 3973
• Main Authors: Dathe, Hannes, Prager, Katja, Mittag, Maria
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 16.11.2012
• Subjects: 5′–3′ exoribonuclease; ADE; adenine; Algal Proteins - genetics; Algal Proteins - metabolism; ambient temperature; Base Sequence; Chlamydomonas reinhardtii; Chlamydomonas reinhardtii - genetics; Chlamydomonas reinhardtii - growth & development; Chlamydomonas reinhardtii - metabolism; Circadian clock; Circadian Clocks - genetics; circadian rhythm; Circadian Rhythm - genetics; Cysteine Proteinase Inhibitors - pharmacology; day–night cycle of 12 h light and 12 h dark; Exonucleases - genetics; Exonucleases - metabolism; GAL4 activation domain; GAL4 DNA-binding domain; GAL4-AD; GAL4-BD; Gene Knockout Techniques; HIS; histidine; Immunoblotting; LEU; leucine; Leupeptins - pharmacology; metabolism; Molecular Sequence Data; Mutation; P-bodies; processing-bodies; proteasome endopeptidase complex; Proteasome Endopeptidase Complex - metabolism; Protein Binding; Protein Subunits - genetics; Protein Subunits - metabolism; Proteolysis; rhythm of chloroplast; RNA; RNA - metabolism; RNA-binding proteins; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism; ROC; Signal Transduction - drug effects; synthetic dropout media; Temperature; TRP; tryptophane; Two-Hybrid System Techniques; untranslated region; UTR; XRN1; XRN1 knock-out mutant; xrn1 mut; GAL4-BD; P-bodies; ADE; GAL4-AD; ROC; Circadian clock; SD; UTR; HIS; TRP; XRN1; xrn1mut; Chlamydomonas reinhardtii; LD; LEU; RNA metabolism
• ISSN: 0014-5793; 1873-3468; 1873-3468
• DOI: 10.1016/j.febslet.2012.09.046

► XRN1 interacts with the C3 subunit of CHLAMY1. ► XRN1 does not significantly interact with the C1 subunit of CHLAMY1. ► XRN1 is degraded by the proteasome pathway. ► XRN1 is increased in cells grown at lower ambient temperature simulating the night. The RNA-binding protein CHLAMY1 of the green alga Chlamydomonas reinhardtii consists of two subunits, named C1 and C3 that maintain the period and phase of the circadian clock. Here, we investigated if any of its subunits interact with other clock components involved in RNA metabolism. We found that C3, but not C1 strongly interacts with exoribonuclease XRN1 whose knockout results in low amplitude rhythms. XRN1 is subject to degradation by the proteasome pathway. Its level increases in cells grown at lower ambient temperature simulating night, which was also observed for C3. Our data indicate a network of clock-relevant RNA-binding proteins. XRN1physically interactswithC3byanti bait coimmunoprecipitation(View interaction)XRN1physically interactswithC3bytwo hybrid(View interaction)C1physically interactswithC3bytwo hybrid(View interaction)