ArticleJournal of bacteriology2005
Import of the transfer RNase colicin D requires site-specific interaction with the energy-transducing protein TonB.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- The Stable Interaction Between Signal Peptidase LepB of Escherichia coli and Nuclease Bacteriocins Promotes Toxin Entry into the Cytoplasm.The Journal of biological chemistry · 2015Article
- Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes.The Journal of biological chemistry · 2012Article
- FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm.The Journal of biological chemistry · 2011Article
- Transcriptional analysis and functional characterization of a gene pair encoding iron-regulated xenocin and immunity proteins of Xenorhabdus nematophila.Journal of bacteriology · 2008Article
- Amino acid starvation and colicin D treatment induce A-site mRNA cleavage in Escherichia coli.Journal of molecular biology · 2008Article
- Deletion and substitution analysis of the Escherichia coli TonB Q160 region.Journal of bacteriology · 2007Article
- Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007Review
- Tol-dependent macromolecule import through the Escherichia coli cell envelope requires the presence of an exposed TolA binding motif.Journal of bacteriology · 2005Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transfer RNase colicin D and ionophoric colicin B appropriate the outer membrane iron siderophore receptor FepA and share a common translocation requirement for the TonB pathway to cross the outer membrane. Despite the almost identical sequences of the N-terminal domains required for the translocation of colicins D and B, two spontaneous tonB mutations (Arg158Ser and Pro161Leu) completely abolished colicin D toxicity but did not affect either the sensitivity to other colicins or the FepA-dependent siderophore uptake capacity. The sensitivity to colicin D of both tonB mutants was fully restored by specific suppressor mutations in the TonB box of colicin D, at Ser18(Thr) and Met19(Ile), respectively. This demonstrates that the interaction of colicin D with TonB is critically dependent on certain residues close to position 160 in TonB and on the side chains of certain residues in the TonB box of colicin D. The effect of introducing the TonB boxes from other TonB-dependent receptors and colicins into colicins D and B was studied. The results of these and other changes in the two TonB boxes show that the role of residues at positions 18 and 19 in colicin D is strongly modulated by other nearby and/or distant residues and that the overall function of colicin D is much more dependent on the interaction with TonB involving the TonB box than is the function of colicin B.
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