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/ The RCAF complex mediates chromatin assembly during DNA replication and repair. The RCAF complex mediates chromatin assembly during DNA replication and repair. Nature (0028-0836) 1999 imex curation Tyler JK., Adams CR., Chen SR., Kobayashi R., Kamakaka RT., Kadonaga JT. Chromatin - Epigenetic interactions resulting in chromatin modulation S190 (190,000g centrifugation) fractions were prepared from Drosophila embryos collected from 0-6 hrs after egg deposition. The purification steps involved SP sepharose column chromatography followed by hydroxyapatite chromatography followed by Mono-S chromatography followed by glycerol gradient centrifugation. jkadonaga@ucsd.edu 12-MAR-2007: Contacted by JYOTI. Only protein-protein interactions drome-embryo drosophilla melanogaster embryo embryo Embryo Defined as the development stage prior to the initiation of tissue differentiation. solution sedimentati cosedimentation in solution solution sedimentati western blot western blot Immuno blot Immuno blot Tyler JK., Adams CR., Chen SR., Kobayashi R., Kamakaka RT., Kadonaga JT. Chromatin - Epigenetic interactions resulting in chromatin modulation S190 (190,000g centrifugation) fractions were prepared from Drosophila embryos collected from 0-6 hrs after egg deposition. The purification steps involved SP sepharose column chromatography followed by hydroxyapatite chromatography followed by Mono-S chromatography followed by glycerol gradient centrifugation. jkadonaga@ucsd.edu Accepted 2007-FEB-21 by DAVET. 12-MAR-2007: Contacted by JYOTI. Nature (0028-0836) 1999 Only protein-protein interactions imex curation The RCAF complex mediates chromatin assembly during DNA replication and repair. The RCAF complex mediates chromatin assembly during DNA replication and repair. Nature (0028-0836) 1999 imex curation Tyler JK., Adams CR., Chen SR., Kobayashi R., Kamakaka RT., Kadonaga JT. Chromatin - Epigenetic interactions resulting in chromatin modulation S190 (190,000g centrifugation) fractions were prepared from Drosophila embryos collected from 0-6 hrs after egg deposition. The purification steps involved SP sepharose column chromatography followed by hydroxyapatite chromatography followed by Mono-S chromatography followed by glycerol gradient centrifugation. jkadonaga@ucsd.edu 12-MAR-2007: Contacted by JYOTI. Only protein-protein interactions drome-embryo drosophilla melanogaster embryo embryo Embryo Defined as the development stage prior to the initiation of tissue differentiation. solution sedimentati cosedimentation in solution solution sedimentati protein sequence protein sequence identification protein sequence Tyler JK., Adams CR., Chen SR., Kobayashi R., Kamakaka RT., Kadonaga JT. Chromatin - Epigenetic interactions resulting in chromatin modulation S190 (190,000g centrifugation) fractions were prepared from Drosophila embryos collected from 0-6 hrs after egg deposition. The purification steps involved SP sepharose column chromatography followed by hydroxyapatite chromatography followed by Mono-S chromatography followed by glycerol gradient centrifugation. S190 (190,000g centrifugation) fractions were prepared from Drosophila embryos collected from 0-6 hrs after egg deposition. The purification steps involved SP sepharose column chromatography followed by hydroxyapatite chromatography followed by Mono-S chromatography followed by glycerol gradient centrifugation. jkadonaga@ucsd.edu Accepted 2007-FEB-21 by DAVET. 12-MAR-2007: Contacted by JYOTI. Nature (0028-0836) 1999 Only protein-protein interactions imex curation h3_drome Histone H3 His3 His3:CG31613 His3:CG33857 His3:CG33860 His3:CG33863 His3:CG33866 CG31613 CG33803 CG33806 CG33809 CG33812 CG33815 CG33818 CG33821 CG33824 CG33827 CG33830 CG33833 CG33836 CG33839 CG33842 CG33845 CG33848 CG33851 CG33854 CG33857 CG33860 CG33863 CG33866 His3:CG33803 His3:CG33806 His3:CG33809 His3:CG33812 His3:CG33815 His3:CG33818 His3:CG33821 His3:CG33824 His3:CG33827 His3:CG33830 His3:CG33833 His3:CG33836 His3:CG33839 His3:CG33842 His3:CG33845 His3:CG33848 His3:CG33851 His3:CG33854 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P02299 original sequence version: 100 6FD8508EA50A0EEC h4_drome Histone H4 H4 His4r H4r CG3379 His4:CG31611 CG31611 His4 His4:CG33869 His4:CG33871 His4:CG33873 His4:CG33875 His4:CG33877 His4:CG33879 His4:CG33881 His4:CG33883 His4:CG33885 His4:CG33887 His4:CG33889 His4:CG33891 His4:CG33893 His4:CG33895 His4:CG33897 His4:CG33899 His4:CG33901 His4:CG33903 His4:CG33905 His4:CG33907 His4:CG33909 CG33869 CG33871 CG33873 CG33875 CG33877 CG33879 CG33881 CG33883 CG33885 CG33887 CG33889 CG33891 CG33893 CG33895 CG33897 CG33899 CG33901 CG33903 CG33905 CG33907 CG33909 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P84040 original sequence version: 97 DIP protein P84040 original sequence version: 36 DIP protein P84040 original sequence version: 50 DF3EB26393BD208C asf1_drome Histone chaperone asf1 asf1 CG9383 Anti-silencing function protein 1 dASF1 Replication-coupling assembly factor subunit ASF1 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MAKVHITNVVVLDNPSSFFNPFQFELTFECIEELKEDLEWKMIYVGSAESEEHDQVLDTIYVGPVPEGRHIFVFQADPPDVSKIPEPDAVGVTIVLLTCSYRGQEFVRVGYYVNNDYADPEMRENPPTKPLFEKLTRNILASKPRVTRFKINWDYGHINGNGNGVENGHQDEMATDGPSTSEAASAVIHPEDDNSLAMPMENGIKALNENSNSLAMEC DIP protein Q9V464 original sequence version: 88 0AD5CA90118BE1C4 asf1-his4 1 3 unspecified role unspecified role neutral component neutral component 4 unspecified role unspecified role neutral component neutral component 5 unspecified role unspecified role neutral component neutral component physical association physical association 1 Three polypeptides were correlated with the peak of RCAF activity through the three final purification steps asf1-his4-1 2 5 unspecified role unspecified role neutral component neutral component 3 unspecified role unspecified role neutral component neutral component lys14 naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain 4 unspecified role unspecified role neutral component neutral component lys5 lys12 naclys N-acetylated L-lysine NAcLys certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain physical association physical association Amino-terminal amino acid sequencing of the smaller RCAF subunits revealed that they are Drosophila histones H3 and H4. Furthermore, this microsequencing analysis indicated that the Lys 5 and Lys 12 of RCAF H4 were acetylated, whereas Lys 8 was not detectably acetylated. Similarly, Lys 14 of RCAF H3 was fully acetylated, whereas Lys 4 and Lys 9 were not detectably acetylated.