Kinetic analysis of morphological differentiation and protease production in Streptomyces albidoflavus SMF301

Kang, Sung Gyun; Lee, Kye Joon

doi:10.1099/00221287-143-8-2709

Cited by 8 publications

(5 citation statements)

References 14 publications

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“…The function of proteases in mammalian systems has been well studied and they are reported to be involved in processes such as the blood clotting cascade, cell cycle, activation of precursor proteins, processing and degradation of proteins and cellular development (for a review, see Travis & Potempa, 2000). Proteases have also been implicated in morphological differentiation and mycelium growth of Streptomyces albidoflavus, a Gram-positive soil bacterium widely known for possessing a variety of hydrolytic enzymes (Kang & Lee, 1997). The expression of the protease gene in this bacterium is found to be dependent upon the proteinaceous nutrients in the environment (Taguchi et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

A new broad-spectrum protease inhibitor from the entomopathogenic bacterium Photorhabdus luminescens

2000

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A new protease inhibitor was purified to apparent homogeneity from a culture medium of Photorhabdus luminescens by ammonium sulfate precipitation and preparative isoelectric focusing followed by affinity chromatography. Ph. luminescens, a bacterium symbiotically associated with the insect-parasitic nematode Heterorhabditis bacteriophora, exists in two morphologically distinguishable phases (primary and secondary). It appears that only the secondary-phase bacterium produces this protease inhibitor. The protease inhibitor has an M r of approximately 12 000 as determined by SDS-PAGE. Its activity is stable over a pH range of 35-11 and at temperatures below 50 SC. The N-terminal 16 amino acids of the protease inhibitor were determined as STGIVTFKND(X)GEDIV and have a very high sequence homology with the N-terminal region of an endogenous inhibitor (IA-1) from the fruiting bodies of an edible mushroom, Pleurotus ostreatus. The purified protease inhibitor inactivated the homologous protease with an almost 1 :1 stoichiometry. It also inhibited proteases from a related insect-nematode-symbiotic bacterium, Xenorhabdus nematophila. Interestingly, when present at a molar ratio of 5 to 1, this new protease inhibitor completely inactivated the activity of both trypsin and elastase. The activity of proteinase A and cathepsin G was partially inhibited by this bacterial protease inhibitor, but it had no effect on chymotrypsin, subtilisin, thermolysin and cathepsins B and D. The newly isolated protease inhibitor from the secondary-phase bacteria and its specific inhibition of its own protease provides an explanation as to why previous investigators failed to detect the presence of protease activity in the secondary-phase bacteria. The functional implications of the protease inhibitor are also discussed in relation to the physiology of nematode-symbiotic bacteria.

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Section: Discussionmentioning

confidence: 99%

A new broad-spectrum protease inhibitor from the entomopathogenic bacterium Photorhabdus luminescens

2000

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“…At the end of growth, TLP activity declines as the mycelium lyses, whereas metalloprotease activity is maintained. In agar‐grown cultures, addition of a TLP inhibitor interferes with aerial growth, while addition of an metalloprotease inhibitor suppresses spore formation (Rho & Lee, 1994; Kang et al , 1995b; Kang & Lee, 1997). It appears that TLP and MTP help to break down substrate mycelium for nutrients to support spore formation (Kang et al , 1998; Lee, 1998).…”

Section: The Roles Of Extracellular Proteases and Protease Inhibitorsmentioning

confidence: 99%

The complex extracellular biology ofStreptomyces

et al. 2010

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Streptomycetes, soil-dwelling mycelial bacteria that form sporulating aerial branches, have an exceptionally large number of predicted secreted proteins, including many exported via the twin-arginine transport system. Their use of noncatalytic substrate-binding proteins and hydrolytic enzymes to obtain soluble nutrients from carbohydrates such as chitin and cellulose enables them to interact with other organisms. Some of their numerous secreted proteases participate in developmentally significant extracellular cascades, regulated by inhibitors, which lead to cannibalization of the substrate mycelium biomass to support aerial growth and sporulation. They excrete many secondary metabolites, including important antibiotics. Some of these play roles in interactions with eukaryotes. Surprisingly, some antibiotic biosynthetic enzymes are extracellular. Antibiotic production is often regulated by extracellular signalling molecules, some of which also control morphological differentiation. Amphipathic proteins, assembled with the help of cellulose-like material, are required for both hyphal attachment to surfaces and aerial reproductive growth. Comparative genomic analysis suggests that the acquisition of genes for extracellular processes has played a huge part in speciation. The rare codon TTA, which is present in the key pleiotropic regulatory gene adpA and many pathway-specific regulatory genes for antibiotic production, has a particular influence on extracellular biology.

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“…However, the different cell types do cooperate. For example, the vegetative mycelium secretes proteases that presumably help break down the substrate mycelium, thereby providing nutrients for sporulation (60,61). In addition, a significant fraction of the vegetative mycelium undergoes cell lysis (61)(62)(63)(64).…”

Section: Bacterial Multicellularity and The Division Of Labormentioning

confidence: 99%

Division of Labor in Biofilms: the Ecology of Cell Differentiation

2015

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The dense aggregation of cells on a surface, as seen in biofilms, inevitably results in both environmental and cellular heterogeneity. For example, nutrient gradients can trigger cells to differentiate into various phenotypic states. Not only do cells adapt physiologically to the local environmental conditions, but they also differentiate into cell types that interact with each other. This allows for task differentiation and, hence, the division of labor. In this article, we focus on cell differentiation and the division of labor in three bacterial species: Myxococcus xanthus, Bacillus subtilis , and Pseudomonas aeruginosa . During biofilm formation each of these species differentiates into distinct cell types, in some cases leading to cooperative interactions. The division of labor and the cooperative interactions between cell types are assumed to yield an emergent ecological benefit. Yet in most cases the ecological benefits have yet to be elucidated. A notable exception is M. xanthus , in which cell differentiation within fruiting bodies facilitates the dispersal of spores. We argue that the ecological benefits of the division of labor might best be understood when we consider the dynamic nature of both biofilm formation and degradation.

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Kinetic analysis of morphological differentiation and protease production in Streptomyces albidoflavus SMF301

Cited by 8 publications

References 14 publications

A new broad-spectrum protease inhibitor from the entomopathogenic bacterium Photorhabdus luminescens

A new broad-spectrum protease inhibitor from the entomopathogenic bacterium Photorhabdus luminescens

The complex extracellular biology ofStreptomyces

Division of Labor in Biofilms: the Ecology of Cell Differentiation

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