Dual roles of the central domain of colicin D tRNase in TonB-mediated import and in immunity
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Dual roles of the central domain of colicin D tRNase in TonB-mediated import and in immunity. / Mora, Liliana; Klepsch, Mirjam; Buckingham, Richard H; Heurgué-Hamard, Valérie; Kervestin, Stephanie; de Zamaroczy, Miklos.
in: J BIOL CHEM, Jahrgang 283, Nr. 8, 22.02.2008, S. 4993-5003.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Dual roles of the central domain of colicin D tRNase in TonB-mediated import and in immunity
AU - Mora, Liliana
AU - Klepsch, Mirjam
AU - Buckingham, Richard H
AU - Heurgué-Hamard, Valérie
AU - Kervestin, Stephanie
AU - de Zamaroczy, Miklos
PY - 2008/2/22
Y1 - 2008/2/22
N2 - Colicin D import into Escherichia coli requires an interaction via its TonB box with the energy transducer TonB. Colicin D cytotoxicity is inhibited by specific tonB mutations, but it is restored by suppressor mutations in the TonB box. Here we report that there is a second site of interaction between TonB and colicin D, which is dependent upon a 45-amino acid region, within the uncharacterized central domain of colicin D. In addition, the 8th amino acids of colicin D (a glycine) and colicin B (a valine), adjacent to their TonB boxes, are also required for TonB recognition, suggesting that high affinity complex formation involves multiple interactions between these colicins and TonB. The central domain also contributes to the formation of the immunity complex, as well as being essential for uptake and thus killing. Colicin D is normally secreted in association with the immunity protein, and this complex involves the following two interactions: a major interaction with the C-terminal tRNase domain and a second interaction involving the central domain of colicin D and, most probably, the alpha4 helix of ImmD, which is on the opposite side of ImmD compared with the major interface. In contrast, formation of the immunity complex with the processed cytotoxic domain, the form expected to be found in the cytoplasm after colicin D uptake, requires only the major interaction. Klebicin D has, like colicin D, a ribonuclease activity toward tRNAArg and a central domain, which can form a complex with ImmD but which does not function in TonB-mediated transport.
AB - Colicin D import into Escherichia coli requires an interaction via its TonB box with the energy transducer TonB. Colicin D cytotoxicity is inhibited by specific tonB mutations, but it is restored by suppressor mutations in the TonB box. Here we report that there is a second site of interaction between TonB and colicin D, which is dependent upon a 45-amino acid region, within the uncharacterized central domain of colicin D. In addition, the 8th amino acids of colicin D (a glycine) and colicin B (a valine), adjacent to their TonB boxes, are also required for TonB recognition, suggesting that high affinity complex formation involves multiple interactions between these colicins and TonB. The central domain also contributes to the formation of the immunity complex, as well as being essential for uptake and thus killing. Colicin D is normally secreted in association with the immunity protein, and this complex involves the following two interactions: a major interaction with the C-terminal tRNase domain and a second interaction involving the central domain of colicin D and, most probably, the alpha4 helix of ImmD, which is on the opposite side of ImmD compared with the major interface. In contrast, formation of the immunity complex with the processed cytotoxic domain, the form expected to be found in the cytoplasm after colicin D uptake, requires only the major interaction. Klebicin D has, like colicin D, a ribonuclease activity toward tRNAArg and a central domain, which can form a complex with ImmD but which does not function in TonB-mediated transport.
KW - Bacteriocins
KW - Escherichia coli
KW - Escherichia coli Proteins
KW - Membrane Proteins
KW - Protein Binding
KW - Protein Structure, Secondary
KW - Protein Structure, Tertiary
KW - Protein Transport
KW - RNA, Transfer, Arg
KW - Ribonucleases
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1074/jbc.M706846200
DO - 10.1074/jbc.M706846200
M3 - SCORING: Journal article
C2 - 18083710
VL - 283
SP - 4993
EP - 5003
JO - J BIOL CHEM
JF - J BIOL CHEM
SN - 0021-9258
IS - 8
ER -