The crystal structure of the dimeric colicin M immunity protein displays a 3D domain swap

Usón, Isabel; Patzer, Silke I.; Rodríguez, Daniel Salazar; Braun, Volkmar; Zeth, Kornelius

doi:10.1016/j.jsb.2012.02.004

Cited by 19 publications

(18 citation statements)

References 41 publications

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“…In E. coli , this is ensured by a coexpressed immunity protein (Cmi) anchored in the cytoplasmic membrane facing the periplasm (Cascales et al ., ). Genes encoding homologs of Cmi or the structurally related YebF protein (Gérard et al ., ; Usón et al ., ) are not found in Pseudomonas genomes.…”

Section: S‐type Pyocinsmentioning

confidence: 97%

Ribosomally encoded antibacterial proteins and peptides fromPseudomonas

2014

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Members of the Pseudomonas genus produce diverse secondary metabolites affecting other bacteria, fungi or predating nematodes and protozoa but are also equipped with the capacity to secrete different types of ribosomally encoded toxic peptides and proteins, ranging from small microcins to large tailocins. Studies with the human pathogen Pseudomonas aeruginosa have revealed that effector proteins of type VI secretion systems are part of the antibacterial armamentarium deployed by pseudomonads. A novel class of antibacterial proteins with structural similarity to plant lectins was discovered by studying antagonism among plant-associated Pseudomonas strains. A genomic perspective on pseudomonad bacteriocinogeny shows that the modular architecture of S pyocins of P. aeruginosa is retained in a large diversified group of bacteriocins, most of which target DNA or RNA. Similar modularity is present in as yet poorly characterized Rhs (recombination hot spot) proteins and CDI (contact-dependent inhibition) proteins. Well-delimited domains for receptor recognition or cytotoxicity enable the design of chimeric toxins with novel functionalities, which has been applied successfully for S and R pyocins. Little is known regarding how these antibacterials are released and ultimately reach their targets. Other remaining issues concern the identification of environmental triggers activating these systems and assessment of their ecological impact in niches populated by pseudomonads.

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Section: S‐type Pyocinsmentioning

confidence: 97%

Ribosomally encoded antibacterial proteins and peptides fromPseudomonas

2014

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“…Moreover, the biological function of the spanin complex requires either the Rz Cys152-RzCys152 or the Rz1Cys29-Rz1Cys29 linkage. There have been very few documented instances of intermolecular disulfide bonds in prokaryotes, all of which were found in proteins of the Gram-negative envelope (Spudich et al, 1996;Klimke et al, 2005;Nagano et al, 2005;Uson et al, 2012). In only one case, with the VirB7 and VirB9 proteins of the Agrobacterium tumefaciens T-complex transport apparatus, have such linkages been shown to be functionally significant.…”

Section: A Covalent Dimer Of Either Rz or Rz1 Is Required For Spanin mentioning

confidence: 99%

Spanin function requires subunit homodimerization through intermolecular disulfide bonds

Berry

Rajaure

Young

2013

Molecular Microbiology

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Summary The λ Rz and Rz1 proteins are the subunits of the spanin complex, required for the disruption of the outer membrane during host lysis. Rz, the inner membrane or i-spanin, has a largely alpha-helical periplasmic domain, whereas Rz1, the outer membrane or o-spanin, has a 25% proline content with no predicted secondary structure. We report that both Rz and Rz1 accumulate as homodimers covalently linked by intermolecular disulfide bonds involving all three Cys residues, two in Rz and one in Rz1. Moreover, of these three intermolecular disulfides, spanin function requires the presence of at least one of the two linkages nearest the Rz-Rz1 C-terminal interaction domains; i.e., either the Rz1-Rz1 disulfide or the distal Rz-Rz disulfide link. In a dsbC host, but not in dsbA or dsbA dsbC hosts, formation of the covalent homodimers of Rz is severely reduced and outer membrane disruption is significantly delayed, suggesting that the spanin pathway normally proceeds through DsbA-mediated formation of an intramolecular disulfide in Rz. In contrast, efficient formation of the Rz1-Rz1 disulfide requires DsbA. Finally, Dsb-independent formation of the covalent homodimer of either subunit requires the presence of the other, presumably as a template for close apposition of the thiols.

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“…In the case of the pore-forming and lipid II-degrading bacteriocins, complex formation with the immunity protein has not been demonstrated. These proteins are localized at the cytoplasmic membrane, where they negate the lethal effects of the toxin by mechanisms that are yet to be clearly delineated (14,15). In general, full protection is afforded only by the cognate immunity protein.…”

mentioning

confidence: 99%

The Crystal Structure of the Lipid II-degrading Bacteriocin Syringacin M Suggests Unexpected Evolutionary Relationships between Colicin M-like Bacteriocins

Grinter

Roszak

Cogdell

et al. 2012

Journal of Biological Chemistry

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Background: Syringacin M is a colicin M-like bacteriocin from the plant-pathogenic species Pseudomonas syringae. Results: The receptor binding domain of syringacin M has unexpected structural homology to that of colicin M. Conclusion: Syringacin M and colicin M appear to have evolved directly from a common ancestor. Significance: Bacteriocins can evolve novel receptor specificities through diversifying selection.

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The crystal structure of the dimeric colicin M immunity protein displays a 3D domain swap

Cited by 19 publications

References 41 publications

Ribosomally encoded antibacterial proteins and peptides fromPseudomonas

Ribosomally encoded antibacterial proteins and peptides fromPseudomonas

Spanin function requires subunit homodimerization through intermolecular disulfide bonds

The Crystal Structure of the Lipid II-degrading Bacteriocin Syringacin M Suggests Unexpected Evolutionary Relationships between Colicin M-like Bacteriocins

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