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Extracellular Streptomyces vesicles: amphorae for survival and defence.

Schrempf H, Koebsch I, Walter S, Engelhardt H, Meschke H - Microb Biotechnol (2011)

Bottom Line: Our LC/MS analyses of generated tryptic peptides led to the identification of distinct proteins that carry often a predicted N-terminal signal peptide with a twin-arginine motif or lack a canonical signal sequence.The proteins are required for a range of processes: the acquisition of inorganic as well as organic phosphate, iron ions, and of distinct carbon sources, energy metabolism and redox balance, defence against oxidants and tellurites, the tailoring of actinorhodin, folding and assembly of proteins, establishment of turgor, and different signalling cascades.Our novel findings have immense implications for understanding new avenues of environmental biology of streptomycetes and for biotechnological applications.

View Article: PubMed Central - PubMed

Affiliation: FB Biology/Chemistry, Applied Genetics of Microorganisms, University Osnabrück, Barbarastr. 13, D-49069 Osnabrück, Germany. schrempf@biologie.uni-osnabrueck.de

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Mentions: Our investigations by transmission electron microscopy (TEM) revealed that droplets contain round and densely packed particles of different size (Fig. 2A). Larger vesicles (diameter 100–250 nm) and smaller particles with defined shapes (diameter 30–80 nm) were present (Fig. 2B and C). The abundance of non‐stainable areas/surfaces on various vesicles was noticeable (Fig. 2C). The presence of vesicles, which had undergone different degrees of disruption, was attributed to their fragility during the process of preparation and negative staining.


Extracellular Streptomyces vesicles: amphorae for survival and defence.

Schrempf H, Koebsch I, Walter S, Engelhardt H, Meschke H - Microb Biotechnol (2011)

© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3818868&req=5

Mentions: Our investigations by transmission electron microscopy (TEM) revealed that droplets contain round and densely packed particles of different size (Fig. 2A). Larger vesicles (diameter 100–250 nm) and smaller particles with defined shapes (diameter 30–80 nm) were present (Fig. 2B and C). The abundance of non‐stainable areas/surfaces on various vesicles was noticeable (Fig. 2C). The presence of vesicles, which had undergone different degrees of disruption, was attributed to their fragility during the process of preparation and negative staining.

Bottom Line: Our LC/MS analyses of generated tryptic peptides led to the identification of distinct proteins that carry often a predicted N-terminal signal peptide with a twin-arginine motif or lack a canonical signal sequence.The proteins are required for a range of processes: the acquisition of inorganic as well as organic phosphate, iron ions, and of distinct carbon sources, energy metabolism and redox balance, defence against oxidants and tellurites, the tailoring of actinorhodin, folding and assembly of proteins, establishment of turgor, and different signalling cascades.Our novel findings have immense implications for understanding new avenues of environmental biology of streptomycetes and for biotechnological applications.

View Article: PubMed Central - PubMed

Affiliation: FB Biology/Chemistry, Applied Genetics of Microorganisms, University Osnabrück, Barbarastr. 13, D-49069 Osnabrück, Germany. schrempf@biologie.uni-osnabrueck.de

Show MeSH
Related in: MedlinePlus