A truncated form of SpoT, including the ACT domain, inhibits the production of cyclic lipopeptide arthrofactin, and is associated with moderate elevation of guanosine 3',5'-bispyrophosphate level in Pseudomonas sp. MIS38
| Autor: | Siew Ping Lim, Kenji Washio, Niran Roongsawang, Masaaki Morikawa |
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| Rok vydání: | 2011 |
| Předmět: |
Transposable element
Transcription Genetic Mutant Molecular Sequence Data Guanosine Guanosine Tetraphosphate Applied Microbiology and Biotechnology Biochemistry Peptides Cyclic Analytical Chemistry Microbiology chemistry.chemical_compound Lipopeptides Transformation Genetic Pseudomonas Amino Acid Sequence RNA Messenger Pyrophosphatases Molecular Biology Sequence Deletion Phenocopy biology Base Sequence Organic Chemistry Biofilm General Medicine biology.organism_classification Null allele Molecular biology Protein Structure Tertiary chemistry Genetic Loci DNA Transposable Elements bacteria ACT domain Biotechnology |
| Zdroj: | Bioscience, biotechnology, and biochemistry. 75(10) |
| ISSN: | 1347-6947 |
| Popis: | Arthrofactin is a biosurfactant produced by Pseudomonas sp. MIS38. We have reported that transposon insertion into spoT (spoT::Tn5) causes moderate accumulation of guanosine 3′,5′-bispyrophosphate (ppGpp) and abrogates arthrofactin production. To analyze the linkage of SpoT function and ablation of arthrofactin production, we examined the spoT::Tn5 mutation. The results showed that spoT::Tn5 is not a null mutation, but encodes separate segments of SpoT. Deletion of the 3′ region of spoT increased the level of arthrofactin production, suggesting that the C-terminal region of SpoT plays a suppressive role. We evaluated the expression of a distinct segment of SpoT. Forced expression of the C-terminal region that contains the ACT domain resulted in the accumulation of ppGpp and abrogated arthrofactin production. Expression of the C-terminal segment also reduced MIS38 swarming and resulted in extensive biofilm formation, which constitutes the phenocopy of the spoT::Tn5 mutant. |
| Databáze: | OpenAIRE |
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