Draft Genome Sequence of
            <i>Streptomyces</i>
            sp. F-3

Sun, Xiaomeng; Meng, Jing; Liu, Shijia; Zhang, Huaiqiang; Wang, Lushan

doi:10.1128/genomea.00780-16

Cited by 2 publications

(2 citation statements)

References 6 publications

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“…The genomes of two Streptomyces isolated from compost are also being sequenced. Both contain a number of interesting polyketide synthase pathways suggesting these strains may produce new compounds [ 226 , 227 ].…”

Section: Bioprospecting For New Polyketide Discoverymentioning

confidence: 99%

Sampling Terrestrial Environments for Bacterial Polyketides

2017

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Bacterial polyketides are highly biologically active molecules that are frequently used as drugs, particularly as antibiotics and anticancer agents, thus the discovery of new polyketides is of major interest. Since the 1980s discovery of polyketides has slowed dramatically due in large part to the repeated rediscovery of known compounds. While recent scientific and technical advances have improved our ability to discover new polyketides, one key area has been under addressed, namely the distribution of polyketide-producing bacteria in the environment. Identifying environments where producing bacteria are abundant and diverse should improve our ability to discover (bioprospect) new polyketides. This review summarizes for the bioprospector the state-of-the-field in terrestrial microbial ecology. It provides insight into the scientific and technical challenges limiting the application of microbial ecology discoveries for bioprospecting and summarizes key developments in the field that will enable more effective bioprospecting. The major recent efforts by researchers to sample new environments for polyketide discovery is also reviewed and key emerging environments such as insect associated bacteria, desert soils, disease suppressive soils, and caves are highlighted. Finally strategies for taking and characterizing terrestrial samples to help maximize discovery efforts are proposed and the inclusion of non-actinomycetal bacteria in any terrestrial discovery strategy is recommended.

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Section: Bioprospecting For New Polyketide Discoverymentioning

confidence: 99%

Sampling Terrestrial Environments for Bacterial Polyketides

2017

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“…Recently, we isolated a thermophilic bacterium Streptomyces sp. F-3 from soil which can grow rapidly at 50 °C [18]. When colloidal chitin was used as the sole carbon substrate, increased chitinase activity was observed.…”

Section: Introductionmentioning

confidence: 99%

A novel thermostable chitinolytic machinery of Streptomyces sp. F-3 consisting of chitinases with different action modes

Sun

Tian

et al. 2019

Biotechnol Biofuels

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Background The biodegradation of chitin is an important part of the carbon and nitrogen cycles in nature. Speeding up the biotransformation of chitin substrates can not only reduce pollution, but also produce high value-added products. However, this process is strictly regulated by the catalytic efficiency of the chitinolytic machinery. Therefore, it is necessary to study the mode of action and compound mechanisms of different chitin-degrading enzymes in depth to improve the catalytic efficiency of the chitinolytic machinery. Results The thermophilic bacterium Streptomyces sp. F-3 showed comparatively high chitin degradation activities. To elucidate the mechanism underlying chitin hydrolysis, six chitin degradation-related enzymes were identified in the extracellular proteome of Streptomyces sp. F-3, including three chitinases ( Ss Chi18A, Ss Chi18B, and Ss Chi18C) from the GH18 family, one GH19 chitinase ( Ss Chi19A), one GH20 β- N -acetylhexosaminidase ( Ss GH20A), and one lytic polysaccharide monooxygenase ( Ss LPMO10A) from the AA10 family. All were upregulated by chitin. The heterologously expressed hydrolases could withstand temperatures up to 70 °C and were stable at pH values of 4 to 11. Biochemical analyses displayed that these chitin degradation-related enzymes had different functions and thus showed synergistic effects during chitin degradation. Furthermore, based on structural bioinformatics data, we speculated that the different action modes among the three GH18 chitinases may be caused by loop differences in their active site architectures. Among them, Ss Chi18A is probably processive and mainly acts on polysaccharides, while Ss Chi18B and Ss Chi18C are likely endo-non-processive and displayed higher activity on the degradation of chitin oligosaccharides. In addition, proteomic data and synergy experiments also indicated the importance of Ss LPMO10A, which could promote the activities of the hydrolases and increase the monosaccharide content in the reaction system, respectively. Conclusions In this article, the chitinolytic machinery of a thermophilic Streptomyces species was studied to explore the structural basis for the synergistic actions of chitinases from different GH18 subfamilies. The elucidation of the degradation mechanisms of these thermophilic chitinases will lay a theoretical foundation for the efficient industrialized transformation of natural chitin. Electronic supplementary material The online version of this article (10.1186/s13068-019-1472-1) contains supplementary material, which is available to authorized ...

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Draft Genome Sequence of Streptomyces sp. F-3

Cited by 2 publications

References 6 publications

Sampling Terrestrial Environments for Bacterial Polyketides

Sampling Terrestrial Environments for Bacterial Polyketides

A novel thermostable chitinolytic machinery of Streptomyces sp. F-3 consisting of chitinases with different action modes

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