Get Bacteriocins: Ecology and Evolution PDF

By Margaret A. Riley, Milind A. Chavan

ISBN-10: 3540366032

ISBN-13: 9783540366034

Microbes produce a rare array of safety platforms. those comprise bacteriocins, a category of antimicrobial molecules with slender killing spectra, produced by way of micro organism. The ebook describes the variety and ecological function of bacteriocins of Gram-positive and Gram-negative micro organism, featuring a brand new class scheme for the previous and a state of the art examine the position of bacteriocins in bacterial communique. It discusses the molecular evolution of colicins and colicin-like bacteriocins, and offers a latest review of archaeocins, bacteriocin-like antimicrobials produced by way of archaebacteria. additionally, numerous modeling (in silico) reports elucidate the function of bacteriocins in microbial group dynamics and health, delving into rock-paper-scissors pageant and the counter-intuitive survival of the weakest. The booklet makes compelling examining for a multi-faceted clinical viewers, together with these operating within the fields of biodiversity and biotechnology, significantly within the human and animal health and wellbeing area.

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Extra info for Bacteriocins: Ecology and Evolution

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2001; Chavan et al. 2005). Similar species-specific diversity is found in their receptor-binding domains. Whereas the associated receptors have been characterized for all colicins, those targeted by CLBs have not been investigated to date. The receptor-binding domains of klebicins C and D have 45% protein sequence similarity to the corresponding domain of colicin D, indicating that these bacteriocins bind to similar proteins in their target species. On the other side of the spectra, the receptor-binding domains of klebicin B, alveicins A and B, and marcescin A are considered to be novel.

Alignments of selected colicin and CLB DNase, rRNase and pore-forming domains are shown in Fig. 5. 2 show percentage similarities and divergence between various pairs of DNase, 16S rRNase and pore-forming colicins respectively. A phylogenetic tree inferred from sequences of nuclease domains of colicins, CLBs and pyocins is 30 Milind A. Chavan and Margaret A. Riley a. DNase killing domains b. DNase immunity proteins Fig. 5 Amino acid alignments of killing domains and immunity proteins of colicins and colicin-like bacteriocins.

Thus, killing domains appear to be transferred more frequently than the targetdefining (specifying) domains for translocation and receptor binding. The CLBs have no (or significantly lower) similarity with well-characterized translocation and receptor-binding domains of colicins, in contrast to that observed for the killing domains (Riley et al. 2001; Wertz and Riley 2004; Chavan et al. 2005). These domains have evolved in CLBs so as to be more adept in exploiting the receptors and translocation mechanisms of their own species.

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Bacteriocins: Ecology and Evolution by Margaret A. Riley, Milind A. Chavan


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