دورية أكاديمية
Cross-talk between type three secretion system and metabolism in Yersinia.
| العنوان: | Cross-talk between type three secretion system and metabolism in Yersinia. |
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| المؤلفون: | Schmid, Annika, Neumayer, Wibke, Trülzsch, Konrad, Israel, Lars, Imhof, Axel, Roessle, Manfred, Sauer, Guido, Richter, Susanna, Lauw, Susan, Eylert, Eva, Eisenreich, Wolfgang, Heesemann, Jürgen, Wilharm, Gottfried |
| بيانات النشر: | Robert Koch-Institut |
| سنة النشر: | 2009 |
| المجموعة: | Robert Koch Institute: Publications |
| مصطلحات موضوعية: | Bacterial Proteins/genetics, Bacterial Proteins/metabolism, Yersinia enterocolitica/genetics, Yersinia enterocolitica/metabolism, Transcription Factors/genetics, Transcription Factors/metabolism, Yersinia enterocolitica/pathogenicity, Glucose/metabolism, Amino Acids/biosynthesis, Amino Acids/genetics, Calcium/metabolism, Calcium/pharmacology, Citric Acid Cycle/drug effects, Citric Acid Cycle/physiology, Glucose/pharmacology, Glycolysis/drug effects, Glycolysis/physiology, Oxaloacetate/metabolism, Phosphoenolpyruvate Carboxylase/genetics, Phosphoenolpyruvate Carboxylase/metabolism, Pyruvic Acid/metabolism, Secretory Pathway/drug effects, Secretory Pathway/physiology, Sweetening Agents/metabolism, Sweetening Agents/pharmacology, 610 Medizin, ddc:610 |
| الوصف: | Pathogenic yersiniae utilize a type three secretion system (T3SS) to inject Yop proteins into host cells in order to undermine their immune response. YscM1 and YscM2 proteins have been reported to be functionally equivalent regulators of the T3SS in Yersinia enterocolitica. Here, we show by affinity purification, native gel electrophoresis and small angle x-ray scattering that both YscM1 and YscM2 bind to phosphoenolpyruvate carboxylase (PEPC) of Y. enterocolitica. Under in vitro conditions, YscM1, but not YscM2, was found to inhibit PEPC with an apparent IC(50) of 4 mum (K(i) = 1 mum). To analyze the functional roles of PEPC, YscM1, and YscM2 in Yop-producing bacteria, cultures of Y. enterocolitica wild type and mutants defective in the formation of PEPC, YscM1, or YscM2, respectively, were grown under low calcium conditions in the presence of [U-(13)C(6)]glucose. The isotope compositions of secreted Yop proteins and nine amino acids from cellular proteins were analyzed by mass spectrometry. The data indicate that a considerable fraction of oxaloacetate used as precursor for amino acids was derived from [(13)C(3)]phosphoenolpyruvate by the catalytic action of PEPC in the wild-type strain but not in the PEPC(-) mutant. The data imply that PEPC is critically involved in replenishing the oxaloacetate pool in the citrate cycle under virulence conditions. In the YscM1(-) and YscM2(-) mutants, increased rates of pyruvate formation via glycolysis or the Entner-Doudoroff pathway, of oxaloacetate formation via the citrate cycle, and of amino acid biosynthesis suggest that both regulators trigger the central metabolism of Y. enterocolitica. We propose a "load-and-shoot cycle" model to account for the cross-talk between T3SS and metabolism in pathogenic yersiniae. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| العلاقة: | http://edoc.rki.de/oa/articles/reMZoJ3jO9FxI/PDF/206O9yAD21mo.pdfTest; http://edoc.rki.de/176904/1345Test; urn:nbn:de:0257-10027777; http://dx.doi.org/10.25646/1270Test |
| DOI: | 10.1074/jbc.M900773200 |
| DOI: | 10.25646/1270 |
| الإتاحة: | https://doi.org/10.1074/jbc.M900773200Test https://doi.org/10.25646/1270Test http://edoc.rki.de/oa/articles/reMZoJ3jO9FxI/PDF/206O9yAD21mo.pdfTest http://edoc.rki.de/176904/1345Test https://nbn-resolving.org/urn:nbn:de:0257-10027777Test |
| رقم الانضمام: | edsbas.4B4A0F42 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1074/jbc.M900773200 |
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