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 A peptide derived from the C-terminus of PB1 inhibits influenza virus replication by interfering with viral polymerase assembly. A peptide derived from the C-terminus of PB1 inhibits influenza virus replication by interfering with viral polymerase assembly. FEBS J. (1742-464X) 2013 Li C., Ba Q., Wu A., Zhang H., Deng T., Jiang T. suggested by lperfetto yeast Saccharomyces cerevisiae Baker's yeast bifc bimolecular fluorescence complementation bifc tag fluorescence tag visualisation by fluorescence tag fluorescence Li C., Ba Q., Wu A., Zhang H., Deng T., Jiang T. suggested by lperfetto FEBS J. (1742-464X) 2013 A peptide derived from the C-terminus of PB1 inhibits influenza virus replication by interfering with viral polymerase assembly. A peptide derived from the C-terminus of PB1 inhibits influenza virus replication by interfering with viral polymerase assembly. FEBS J. (1742-464X) 2013 Li C., Ba Q., Wu A., Zhang H., Deng T., Jiang T. suggested by lperfetto in vitro In vitro pull down pull down experimental particp experimental participant identification experimental particp Li C., Ba Q., Wu A., Zhang H., Deng T., Jiang T. suggested by lperfetto FEBS J. (1742-464X) 2013 rdrp_i96a0 RNA-directed RNA polymerase catalytic subunit PB1 Polymerase basic protein 1 RNA-directed RNA polymerase subunit P1 protein protein i96a0 Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd) MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGKWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCLETMEVVQQTRVDKLTQGRQTYDWTLKRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMDKGEMEIITHFQRKRRVRDNMTKKMVTQRTIGKKKQRLNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLASIDLKYFNESTRKKIEKIRPLLIDGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFALIVNAPNHEGIEAGVDRFYRTCKLVGINMTKKKSYINRTGTCEFTSFFYRYGFVANFSMELPSFGVSGINESADMSIGVTVIKNNMMDNDLGPATAQMALQLFIKDYRYPYRCHRGDTQIQTRRSFELKKLWEQTRSKAGLLVSDGGPNPYNIRNLHIPEAGLKWELMDEDYQGRLCNPLNPFVSHKEIESVNNAVVMPAHGPAKSMEYDAVATTHSWIPKRNRSILNTSQRGILEDEQMYQKCCNLFEKFFPSSSYRRPVGISSMVEAMVSRARIDARIDFESGRIKKEEFAEIMKICSTIEELGRQK DIP protein Q9Q0V0 original sequence version: 54 mint homomint D3F07429E0421159 pb2_i96a0 Polymerase basic protein 2 PB2 RNA-directed RNA polymerase subunit P3 protein protein i96a0 Influenza A virus (strain A/Goose/Guangdong/1/1996 H5N1 genotype Gs/Gd) MERIKELRDLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRIMEMIPERNEQGQTLWSKTNDAGSDRVMVSPLAVTWWNRNGPTTSTVHYPKVYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKIAPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRATVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTNGSSVKKEEEVLTGNLQTLKIKVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGIEPIDNVMGMIGILPDMTPSAEMSLRGVRVSKMGVDEYSSTERVVVSIDRFLRVRDQQGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQDPTMLYNKMEFESFQSLVPKAARSQYSGFVRTLFQQMRDVLGTFDTVQIIKLLPFAAAPPEPSRMQFSSLTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGALTEDPDEGTAGVESAVLRGFLILGREDKRYGPALSINELSNLAKGEKANVLIMQGDVVLVMKRKRDFSILTDSQTATKRIRMAIN mint homomint F9C2D08303F2786D pb1-pb2-4 1 PB1c 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain PB2n 4 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association homomint mint f1a t1 The interaction between YN-PB2n YC-PB1c was significantly disrupted when the self competitor PB1c was expressed in the yeast cells while it was not interfered in the presence of an unrelated peptide PX or in the absence of the peptides. pb1-pb1-2 1 PB1 (731-757) 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9Q0V0:p.Ile750Asn mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I N Tue Jul 12 10:06:57 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:38:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile750asn' Tue Jun 30 20:16:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile750Asn' binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain PB1c 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association t1 homomint mint As shown in Table 2, the mutations of the hydrophobic residues can significantly affect the interaction of PB1c with PB1731-757: L695D and M718A substitutions completely abolished PB1c-PB1731-757 interaction, F699A and I750N/I750D mutations resulted in a much lower binding capacity. In contrast, the mutations of the hydrophilic amino acids R727 and K745 did not affect the binding. Together, it indicates that the hydrophobic residues of all three helixes of PB1c are essential for the PB1c-PB1731-757 interaction. pb1-pb1-3 1 PB1c 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell Q9Q0V0:p.Ile750Asx mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I B Tue Jul 12 10:18:31 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 19:34:10 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile750asx' Tue Jun 30 19:17:02 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile750Asx' yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain PB1 (731-757) 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association homomint mint t1 t2 As shown in Table 2, the mutations of the hydrophobic residues can significantly affect the interaction of PB1c with PB1731-757: L695D and M718A substitutions completely abolished PB1c-PB1731-757 interaction, F699A and I750N/I750D mutations resulted in a much lower binding capacity. In contrast, the mutations of the hydrophilic amino acids R727 and K745 did not affect the binding. Together, it indicates that the hydrophobic residues of all three helixes of PB1c are essential for the PB1c-PB1731-757 interaction. pb1-pb1-4 1 PB1 (731-757) 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain PB1c 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q9Q0V0:p.Phe699Ala mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A Tue Jul 12 10:18:20 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 16:33:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe699ala' Tue Jun 30 17:26:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe699Ala' physical association physical association homomint mint t1 t2 As shown in Table 2, the mutations of the hydrophobic residues can significantly affect the interaction of PB1c with PB1731-757: L695D and M718A substitutions completely abolished PB1c-PB1731-757 interaction, F699A and I750N/I750D mutations resulted in a much lower binding capacity. In contrast, the mutations of the hydrophilic amino acids R727 and K745 did not affect the binding. Together, it indicates that the hydrophobic residues of all three helixes of PB1c are essential for the PB1c-PB1731-757 interaction. pb1-pb1-5 1 PB1c 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9Q0V0:p.Leu695Asp mutation decreasing interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L D Tue Jul 12 10:18:52 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 15:57:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu695asp' Tue Jun 30 15:39:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu695Asp' binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain PB1 (731-757) 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association homomint mint t1 t2 As shown in Table 2, the mutations of the hydrophobic residues can significantly affect the interaction of PB1c with PB1731-757: L695D and M718A substitutions completely abolished PB1c-PB1731-757 interaction, F699A and I750N/I750D mutations resulted in a much lower binding capacity. In contrast, the mutations of the hydrophilic amino acids R727 and K745 did not affect the binding. Together, it indicates that the hydrophobic residues of all three helixes of PB1c are essential for the PB1c-PB1731-757 interaction. pb1-pb1-6 1 PB1 (731-757) 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain PB1c 3 tag fluorescence tag visualisation by fluorescence tag fluorescence experimental particp experimental participant identification experimental particp unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed living cell living cell binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain yfp tag yfp tag yellow fluorescent protein tag YFP yellow fluorescent protein yellow fluorescent protein YFP yfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9Q0V0:p.Met718Ala mutation decreasing interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain M A Tue Jul 12 10:21:09 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation decreasing' Wed May 02 19:59:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met718ala' Tue Jun 30 16:35:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met718Ala' physical association physical association homomint mint t1 t2 As shown in Table 2, the mutations of the hydrophobic residues can significantly affect the interaction of PB1c with PB1731-757: L695D and M718A substitutions completely abolished PB1c-PB1731-757 interaction, F699A and I750N/I750D mutations resulted in a much lower binding capacity. In contrast, the mutations of the hydrophilic amino acids R727 and K745 did not affect the binding. Together, it indicates that the hydrophobic residues of all three helixes of PB1c are essential for the PB1c-PB1731-757 interaction. pb2-pb1 2 PB1c 3 anti tag western anti tag western blot anti tag western experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain mbp tag mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined PB2n 4 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain gst tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association homomint mint f1b f2a f2b Fig. 1B shows that the pull-down efficiency of MBP-tagged PB1c (MBP-PB1c) by GST-tagged PB2n (GST-PB2n) can be significantly affected by the presence of PB1731-757, in comparison with the presence of the control peptide PX while PB1731-757I750N showed less inhibitory effect. pb1-pb1-7 2 PB1 (731-757) 3 predetermined predetermined participant predetermined experimental particp experimental participant identification experimental particp unspecified role unspecified role bait bait purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q9Q0V0:p.Ile750Asn mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain I N Tue Jul 12 10:21:28 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 17:45:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile750asn' Tue Jun 30 16:53:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile750Asn' gst tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined PB1c 3 anti tag western anti tag western blot anti tag western experimental particp experimental participant identification experimental particp unspecified role unspecified role prey prey over-expressed over expressed level over-expressed cell lysate cell lysate mbp tag mbp tag maltose binding protein tag maltose binding protein tag maltose binding protein tag mbp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain physical association physical association homomint mint As shown in Fig. 2D, both deletion of N- terminal 6 amino acids (PB1737-757) and then C- terminal 5 amino acids (PB1737-752) drastically disrupted that PB1c binding capacity suggesting PB1731-757 is the minimal sequence requirement for the PB1c binding capacity. Therefore, we concluded that full-length PB1c is required for its interaction with PB1731-757 f2b f2d f3