An abundance of bacterial ADP-ribosyltransferases — implications for the origin of exotoxins and their human homologues
作者： Mark J Pallen , Alex C Lam , Nicholas J Loman , Alan McBride
DOI: 10.1016/S0966-842X(01)02074-1
关键词:
摘要: ADP-ribosylation is a post-translational modification that can be seen in many contexts, including as the primary mechanism of action important bacterial exotoxins. By data-mining complete and incomplete genome sequences, we have discovered >20 novel putative ADP-ribosyltransferases, several new potential toxins.
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sci-hub.se 参考文章(33)
A.G. Murzin, OB(oligonucleotide/oligosaccharide binding)-fold : common structural and functional solution for non-homologous sequences The EMBO Journal. ,vol. 12, pp. 861- 867 ,(1993) , 10.1002/J.1460-2075.1993.TB05726.X
Kai Wilkens, Bernd Tiemann, Fernando Bazan, Wolfgang Rüger, ADP-Ribosylation and Early Transcription Regulation by Bacteriophage T4 Advances in Experimental Medicine and Biology. ,vol. 419, pp. 71- 82 ,(1997) , 10.1007/978-1-4419-8632-0_8
J. Fernando Bazan, Friedrich Koch-Nolte, Sequence and Structural Links between Distant ADP-Ribosyltransferase Families Advances in Experimental Medicine and Biology. ,vol. 419, pp. 99- 107 ,(1997) , 10.1007/978-1-4419-8632-0_12
John A. Tainer, Seungil Han, Joyce A. Craig, Christopher D. Putnam, Nadine B. Carozzi, Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex. Nature Structural & Molecular Biology. ,vol. 6, pp. 932- 936 ,(1999) , 10.1038/13300
Y. Xu, V. Barbançon-Finck, J.T. Barbieri, Role of histidine 35 of the S1 subunit of pertussis toxin in the ADP-ribosylation of transducin Journal of Biological Chemistry. ,vol. 269, pp. 9993- 9999 ,(1994) , 10.1016/S0021-9258(17)36980-6
R. Antoine, C. Locht, The NAD-glycohydrolase activity of the pertussis toxin S1 subunit. Involvement of the catalytic HIS-35 residue. Journal of Biological Chemistry. ,vol. 269, pp. 6450- 6457 ,(1994) , 10.1016/S0021-9258(17)37393-3
M H Serres, J C Ensign, Endogenous ADP-ribosylation of proteins in Mycobacterium smegmatis. Journal of Bacteriology. ,vol. 178, pp. 6074- 6077 ,(1996) , 10.1128/JB.178.20.6074-6077.1996
M Sugai, K Hashimoto, A Kikuchi, S Inoue, H Okumura, K Matsumoto, Y Goto, H Ohgai, K Moriishi, B Syuto, Epidermal cell differentiation inhibitor ADP-ribosylates small GTP-binding proteins and induces hyperplasia of epidermis. Journal of Biological Chemistry. ,vol. 267, pp. 2600- 2604 ,(1992) , 10.1016/S0021-9258(18)45923-6
Yuko Matsushima-Hibiya, Masahiko Watanabe, Takuo Kono, Takashi Kanazawa, Kotaro Koyama, Takashi Sugimura, Keiji Wakabayashi, Purification and cloning of pierisin-2, an apoptosis-inducing protein from the cabbage butterfly, Pieris brassicae. FEBS Journal. ,vol. 267, pp. 5742- 5750 ,(2000) , 10.1046/J.1432-1327.2000.01640.X
C Locht, A proposed mechanism of ADP-ribosylation catalyzed by the pertussis toxin S1 subunit Biochimie. ,vol. 77, pp. 333- 340 ,(1995) , 10.1016/0300-9084(96)88143-0