MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Novel interaction of two clock-relevant RNA-binding proteins C3 and XRN1 in Chlamydomonas reinhardtii. Novel interaction of two clock-relevant RNA-binding proteins C3 and XRN1 in Chlamydomonas reinhardtii. FEBS Lett. (0014-5793) 2012 Dathe H., Prager K., Mittag M. yeast Saccharomyces cerevisiae Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Dathe H., Prager K., Mittag M. FEBS Lett. (0014-5793) 2012 Novel interaction of two clock-relevant RNA-binding proteins C3 and XRN1 in Chlamydomonas reinhardtii. Novel interaction of two clock-relevant RNA-binding proteins C3 and XRN1 in Chlamydomonas reinhardtii. FEBS Lett. (0014-5793) 2012 Dathe H., Prager K., Mittag M. chlre Chlamydomonas reinhardtii Chlamydomonas smithii anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Dathe H., Prager K., Mittag M. FEBS Lett. (0014-5793) 2012 a8j1z6_chlre XRN1 CHLREDRAFT_95232 protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MGIPKFYRWLSERYPLLNQKLTLTEGPPEMDNLYLDMNGIIHNCTHANRKDIGGVTEEDMMLKVFDYLDKLVQIVRPQKLLFMAIDGVAPRAKMNQQRSRRFKSAMERLKNEEEQRRKGEVVPDDAFDSNCITPGTEFMARLGKHLRFFIRRKMAEDPLWQKPNVVFSGRN mint 24CADCB1D111236C a8hyr6_chlre CRB1 CHLREDRAFT_182403 protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MADHEEPPPGTYDGEERAPDVETGNSHLPPPPELHAAPQEHGADQGAVLDAGRSRAEMLAAIFAAQAGANVVPSDPTGHKRKLDDDEYHDAPDSKRPASMAFGDGSGALPPPPPLGADAPVAMETIMCPPDKVGRVIGRAGATIRDLEASTGTRIQVDHKAPGDKPVTISGRADEVERAKRQVLDLISGHGSDAAPAPGEAQKTLECPQGIVGRVIGRGGETIRTLQQASGAHILVNQDFPEGAARQITISGSQDAVDRAASMVQELIGGEHANTSQVVQRFGVGSTEVLECPKTMVGRIIGKGGETIKDLQKRFNASIQIDQSAMPCKVTITGPSHTIASARRAIEDLIRSTGPPPGGMGMGGGSRPPYGAPYGQQYPGGAGGYGGGYGGYGAPGGYGAPGGYPGYGGYGGYPGGAPYGGYNAGGYGAPGAQSSDPYGAGSSSYNYGGAGGGSSSAAPGAPGSTPAAPGTNGSGSGGSSPWQALQDDQGRTYYYNSTTGVSQWERPADMP mint FF70E3B50BD35DDA q6rbz0_chlre protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii EAELAIEHENGTANLGGGRTLLVKFADPPRGRGDGPVMGVAPKKLFVGQIPQHTTEQHIRSLFAPFGNITDVHVLNKGNAPGCAFVTYERWAHAEAAMLSLNGQTLIEGATTPMVVKFADAKVQDMGGQKRGFGAVEGAPPGVFPGAAAGPGGNKRTFTGAGAPGAMGMAGMAAAGYNPYAAAAAMGYDMSTMAAMGYGNMGMMAGMAGMQQGIPGQGGQQGMGGGAMGGAGAMGGAQGLGAGGMGGMGGMGGMGGGLMAGMNMMGLGMGGGMGMNKPGLQEGPKAWKLFIGQVPFEANETDLWPIFSPLGNILELVILRHQGKSKGCAFLTYENRTDAEKAIRTLDSQVSVPSDPRGRLLTVKYANSAAAAAM mint D4AA31D21B3995BD xrn1-q6rbz0 1 C3 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined XRN1 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f1 mint these data clearly suggest that XRN1 is a strong interaction partner of C3, they only point to C1 as a potential weak interaction partner if at all. crb1-q6rbz0 1 C1 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined C3 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role prey prey over-expressed over expressed level over-expressed living cell living cell fusion protein fusion protein fusion protein undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association f1 mint The interaction of C1 and C3 had first been identified by biochemical assays including immunoprecipitation [2]. Here, it was confirmed using the yeast two-hybrid studies (Fig. 1). xrn1-q6rbz0-1 2 XRN1 3 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level C3 5 western blot western blot Immuno blot Immuno blot predetermined predetermined participant predetermined unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association f3 mint We double-checked the interaction between XRN1 and C3 or C1 by co-immunoprecipitation with purified anti-XRN1 antibodies (see Methods) using proteins of crude extracts of 4A+ cells and cells from xrn1mut (negative control), respectively. As expected, XRN1 was detected in the eluate from the co-immunoprecipitation assay along with 4A+ cells, in contrast to cells of xrn1mut. In addition, C3 was found in the eluate of 4A+ cells by immunoblots with anti-C3 antibodies, but not in the negative control (Fig. 3). C1 was not detected in the eluates of either 4A+ or xrn1mut. These data confirm that XRN1 interacts with the C3 subunit of CHLAMY1, but it does not interact with C1 at a significant rate.