The formation of the rodlet layer of streptomycetes is the result of the interplay between rodlins and chaplins

Claessen, Dennis; Stokroos, I.; Deelstra, Heine J.; Penninga, Nynke A.; Bormann, Christiane; Salas, José Valero; Dijkhuizen, Lubbert; Wösten, Han A. B.

doi:10.1111/j.1365-2958.2004.04143.x

Cited by 125 publications

(170 citation statements)

References 35 publications

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“…As mixtures of ChpD to -H isolated from cell walls of aerial hyphae are highly surface active (29), it is presumed that these proteins would lower the water surface tension and thus allow the emergence of aerial hyphae at the air-water interface. In this model, the large chaplins ChpA to -C would be anchored by sortase to the bacterial peptidoglycan and would serve as a scaffold for the assembly of the small chaplins ChpD to -H. In addition, the chaplin layer provides a hydrophobic surface for the formation of the RdlA-RdlB rodlet layer, the highly insoluble, outer layer of proteins that facilitate spore dispersion (30).…”

Section: Hyphal Development In Streptomyces Coelicolormentioning

confidence: 99%

Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria

Marraffini

DeDent²,

Schneewind³

2006

Microbiol Mol Biol Rev

608

600

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SUMMARY The cell wall envelopes of gram-positive bacteria represent a surface organelle that not only functions as a cytoskeletal element but also promotes interactions between bacteria and their environment. Cell wall peptidoglycan is covalently and noncovalently decorated with teichoic acids, polysaccharides, and proteins. The sum of these molecular decorations provides bacterial envelopes with species- and strain-specific properties that are ultimately responsible for bacterial virulence, interactions with host immune systems, and the development of disease symptoms or successful outcomes of infections. Surface proteins typically carry two topogenic sequences, i.e., N-terminal signal peptides and C-terminal sorting signals. Sortases catalyze a transpeptidation reaction by first cleaving a surface protein substrate at the cell wall sorting signal. The resulting acyl enzyme intermediates between sortases and their substrates are then resolved by the nucleophilic attack of amino groups, typically provided by the cell wall cross bridges of peptidoglycan precursors. The surface protein linked to peptidoglycan is then incorporated into the envelope and displayed on the microbial surface. This review focuses on the mechanisms of surface protein anchoring to the cell wall envelope by sortases and the role that these enzymes play in bacterial physiology and pathogenesis.

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Section: Hyphal Development In Streptomyces Coelicolormentioning

confidence: 99%

Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria

Marraffini

DeDent²,

Schneewind³

2006

Microbiol Mol Biol Rev

608

600

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“…Genes to the left of orf1 are predicted to be involved in mycothiol detoxification, and no function in cypemycin biosynthesis is envisaged. Genes downstream of cypI encode rodlins and a chaplin (homologs of SCO2716 to SCO2719) (10) that have been implicated in morphological development in S. coelicolor (15) and therefore also are unlikely to be involved in cypemycin biosynthesis.…”

Section: Identification Of the Cypemycin Biosynthetic Gene Cluster Rementioning

confidence: 99%

Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides

Claesen

Bibb

2010

Proc. Natl. Acad. Sci. U.S.A.

133

203

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Posttranslational modification of amino acids confers a range of structural features and activities on ribosomally synthesized peptides, many of which have potent antimicrobial or other biological activities. Cypemycin is an extensively modified linear peptide produced by Streptomyces sp. OH-4156 with potent in vitro activity against mouse leukemia cells. Cypemycin does not contain lanthionine bridges but exhibits some of the structural features of lantibiotics, notably dehydrated threonines (dehydrobutyrines) and a C-terminal S-[(Z)-2-aminovinyl]-D-cysteine. Consequently it was classified as a member of the lantibiotic family of posttranslationally modified peptides. Cypemycin also possesses two L-allo-isoleucine residues and an N-terminal N,N-dimethylalanine, both unique amino acid modifications. We identified and heterologously expressed the cypemycin biosynthetic gene cluster and performed a mutational analysis of each individual gene. We show that even the previously described modifications are carried out by unusual enzymes or via a modification pathway unrelated to lantibiotic biosynthesis. Bioinformatic analysis revealed the widespread occurrence of cypemycinlike gene clusters within the bacterial kingdom and in the Archaea. Cypemycin is the founding member of an unusual class of posttranslationally modified ribosomally synthesized peptides, the linaridins.Actinomycetes | antibiotic | enzymology | natural products | Streptomyces

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“…The chaplins consist of eight members, ChpA to ChpH, that self-assemble into amyloid fibrils (7,11). In addition, the rodlin proteins, RdlA and RdlB, are believed to organize chaplin fibrils into "rodlets" (8). When grown on rich medium, S. coelicolor also secretes a lantibiotic-like peptide, SapB (17), which lowers the medium surface tension and is thought to enable hyphae to breach the medium-air interface to grow into the air (21).…”

mentioning

confidence: 99%

Characterization of Changes to the Cell Surface during the Life Cycle of Streptomyces coelicolor : Atomic Force Microscopy of Living Cells

et al. 2007

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Cell surface changes that accompany the complex life cycle of Streptomyces coelicolor were monitored by atomic force microscopy (AFM) of living cells. Images were obtained using tapping mode to reveal that young, branching vegetative hyphae have a relatively smooth surface and are attached to an inert silica surface by means of a secreted extracellular matrix. Older hyphae, representing a transition between substrate and aerial growth, are sparsely decorated with fibers. Previously, a well-organized stable mosaic of fibers, called the rodlet layer, coating the surface of spores has been observed using electron microscopy. AFM revealed that aerial hyphae, prior to sporulation, possess a relatively unstable dense heterogeneous fibrous layer. Material from this layer is shed as the hyphae mature, revealing a more tightly organized fibrous mosaic layer typical of spores. The aerial hyphae are also characterized by the absence of the secreted extracellular matrix. The formation of sporulation septa is accompanied by modification to the surface layer, which undergoes localized temporary disruption at the sites of cell division. The characteristics of the hyphal surfaces of mutants show how various chaplin and rodlin proteins contribute to the formation of fibrous layers of differing stabilities. Finally, older spores with a compact rodlet layer develop surface concavities that are attributed to a reduction of intracellular turgor pressure as metabolic activity slows.The model organism Streptomyces coelicolor represents a group of soil-dwelling filamentous bacteria responsible for synthesis of a wide range of bioactive secondary metabolites, in particular, antibiotics. A good understanding of streptomycete biology has been established, based on extensive studies of S. coelicolor over many years and, more recently, availability of this bacterium's complete genome sequence (1). Of particular interest is the complex streptomycete life cycle. After spore germination, vegetative growth leads to formation of a mycelium consisting of a ramifying network of syncytial hyphae that penetrate a moist substrate by extension of hyphal tips and subapical branching. Subsequent reproductive growth often coincides with the onset of antibiotic production and proceeds with the formation of filamentous aerial hyphae that eventually undergo differentiation into chains of unigenomic spores. Several genes that are critical to various stages of this morphological differentiation have been described in S. coelicolor (5, 15), including bld genes, required for the initial growth of aerial hyphae, and whi genes, needed for the subsequent development of spore chains. Growth into the air is accompanied by a change in cell surface properties: vegetative hyphae growing in moist substrates have hydrophilic cell surfaces, whereas the aerial hyphae and spores are hydrophobic.

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The formation of the rodlet layer of streptomycetes is the result of the interplay between rodlins and chaplins

Cited by 125 publications

References 35 publications

Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria

Sortases and the Art of Anchoring Proteins to the Envelopes of Gram-Positive Bacteria

Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides

Characterization of Changes to the Cell Surface during the Life Cycle of Streptomyces coelicolor : Atomic Force Microscopy of Living Cells

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