IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ CEO1, a new protein from Arabidopsis thaliana, protects yeast against oxidative damage. CEO1, a new protein from Arabidopsis thaliana, protects yeast against oxidative damage. FEBS Lett. (0014-5793) 2000 imex curation Belles-Boix E., Babiychuk E., Van Montagu M., Inze D., Kushnir S. The authors mention a protein that was homologous to a large group of proteins that contain the DNA-binding motif AP2. In particular, the strongest homology was found in the DNA-binding domain of several related to AP2 (RAP2) proteins from Arabidopsis and EREBP proteins from Nicotiana tabacum. However they do not provide an accession number or nucleotide/amino acid sequence of the protein. It was not possible to identify this protein and is therefore not curated in this entry. diinz@gengenp.rug.ac.be 16-Dec-2008: Contacted by JYOTI. Arabidopsis cDNA library made from 3 week old seedlings orchard Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) 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 Belles-Boix E., Babiychuk E., Van Montagu M., Inze D., Kushnir S. The authors mention a protein that was homologous to a large group of proteins that contain the DNA-binding motif AP2. In particular, the strongest homology was found in the DNA-binding domain of several related to AP2 (RAP2) proteins from Arabidopsis and EREBP proteins from Nicotiana tabacum. However they do not provide an accession number or nucleotide/amino acid sequence of the protein. It was not possible to identify this protein and is therefore not curated in this entry. The authors mention a protein that was homologous to a large group of proteins that contain the DNA-binding motif AP2. In particular, the strongest homology was found in the DNA-binding domain of several related to AP2 (RAP2) proteins from Arabidopsis and EREBP proteins from Nicotiana tabacum. However they do not provide an accession number or nucleotide/amino acid sequence of the protein. It was not possible to identify this protein and is therefore not curated in this entry. diinz@gengenp.rug.ac.be Accepted 2008-Not a month!-2 by ORCHARD. 16-Dec-2008: Contacted by JYOTI. Arabidopsis cDNA library made from 3 week old seedlings FEBS Lett. (0014-5793) 2000 orchard Only protein-protein interactions imex curation CEO1, a new protein from Arabidopsis thaliana, protects yeast against oxidative damage. CEO1, a new protein from Arabidopsis thaliana, protects yeast against oxidative damage. FEBS Lett. (0014-5793) 2000 imex curation Belles-Boix E., Babiychuk E., Van Montagu M., Inze D., Kushnir S. The authors mention a protein that was homologous to a large group of proteins that contain the DNA-binding motif AP2. In particular, the strongest homology was found in the DNA-binding domain of several related to AP2 (RAP2) proteins from Arabidopsis and EREBP proteins from Nicotiana tabacum. However they do not provide an accession number or nucleotide/amino acid sequence of the protein. It was not possible to identify this protein and is therefore not curated in this entry. diinz@gengenp.rug.ac.be 16-Dec-2008: Contacted by JYOTI. Arabidopsis cDNA library made from 3 week old seedlings orchard Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) 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 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Belles-Boix E., Babiychuk E., Van Montagu M., Inze D., Kushnir S. The authors mention a protein that was homologous to a large group of proteins that contain the DNA-binding motif AP2. In particular, the strongest homology was found in the DNA-binding domain of several related to AP2 (RAP2) proteins from Arabidopsis and EREBP proteins from Nicotiana tabacum. However they do not provide an accession number or nucleotide/amino acid sequence of the protein. It was not possible to identify this protein and is therefore not curated in this entry. diinz@gengenp.rug.ac.be Accepted 2008-Not a month!-2 by ORCHARD. 16-Dec-2008: Contacted by JYOTI. Arabidopsis cDNA library made from 3 week old seedlings FEBS Lett. (0014-5793) 2000 orchard Only protein-protein interactions imex curation rcd1_arath Inactive poly [ADP-ribose] polymerase RCD1 RCD1 ATP8 CEO1 Protein RADICAL-INDUCED CELL DEATH 1 F3C3.1 At1g32230 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MEAKIVKVLDSSRCEDGFGKKRKRAASYAAYVTGVSCAKLQNVPPPNGQCQIPDKRRRLEGENKLSAYENRSGKALVRYYTYFKKTGIAKRVMMYENGEWNDLPEHVICAIQNELEEKSAAIEFKLCGHSFILDFLHMQRLDMETGAKTPLAWIDNAGKCFFPEIYESDERTNYCHHKCVEDPKQNAPHDIKLRLEIDVNGGETPRLNLEECSDESGDNMMDDVPLAQRSSNEHYDEATEDSCSRKLEAAVSKWDETDAIVVSGAKLTGSEVLDKDAVKKMFAVGTASLGHVPVLDVGRFSSEIAEARLALFQKQVEITKKHRGDANVRYAWLPAKREVLSAVMMQGLGVGGAFIRKSIYGVGIHLTAADCPYFSARYCDVDENGVRYMVLCRVIMGNMELLRGDKAQFFSGGEEYDNGVDDIESPKNYIVWNINMNTHIFPEFVVRFKLSNLPNAEGNLIAKRDNSGVTLEGPKDLPPQLESNQGARGSGSANSVGSSTTRPKSPWMPFPTLFAAISHKVAENDMLLINADYQQLRDKKMTRAEFVRKLRVIVGDDLLRSTITTLQNQPKSKEIPGSIRDHEEGAGGL DIP protein Q8RY59 original sequence version: 81 1803D75683524CDC bbx24_arath B-box zinc finger protein 24 BBX24 STO Salt tolerance protein T21E18.8 T21E18.9 At1g06040 protein protein arath Arabidopsis thaliana (Mouse-ear cress) Mouse-ear cress MKIQCDVCEKAPATVICCADEAALCPQCDIEIHAANKLASKHQRLHLNSLSTKFPRCDICQEKAAFIFCVEDRALLCRDCDESIHVANSRSANHQRFLATGIKVALTSTICSKEIEKNQPEPSNNQQKANQIPAKSTSQQQQQPSSATPLPWAVDDFFHFSDIESTDKKGQLDLGAGELDWFSDMGFFGDQINDKALPAAEVPELSVSHLGHVHSYKPMKSNVSHKKPRFETRYDDDDEEHFIVPDLG 4E7A960D56741B0A ceo1-sto 2 3 unspecified role unspecified role bait bait 4 unspecified role unspecified role prey prey physical association physical association One of the cDNAs encoded the protein STO (X95572) from A. thaliana, a protein that confers salt tolerance to yeast [20]. STO is highly similar to putative zinc finger-containing proteins, such as CO (Gi 2695703). ceo1-sto-1 1 3 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role prey prey physical association physical association Next, we carried out the deletion analysis of the CEO1-coding sequence. The two-hybrid assay was also used to identify domains of interaction of CEO1 with its preys. For this purpose, five deletions in the coding region of CEO1 were generated by PCR (see Section 2) and cloned into the pGBT9 vector as carboxyl-terminal fusions with the DNA-binding domain of GAL4. Yeast HF7c was transformed with all combinations of the CEO1 deletions and the isolated preys. The protein�protein interactions were assessed by growth of the transformants in SD His− medium with or without 20 mM AT and by subsequent β-galactosidase staining. As summarized in Fig. 5, the interacting domain of CEO1 was located in its carboxyl-terminal part, between the amino acids 345 and 589. Figure 5