Unsere AG beschäftigt sich mit dem Metabolismus von Biopolymeren in Mikroorganismen: (i) Polyhydroxybuttersäue(PHB) und verwandte Polyhydroxyalkanoate (PHAs) werden von vielen Bakterien als Speicherstoffe in Form von PHA Granula synthetisiert. PHAs sind sog. „Biokunststoffe“ und gelten aufgrund ihrer Bioabbaubarkeit zu H2O und CO2 und Synthese aus nachwachsenden Rohstoffen als umweltfreundliche Alternativen zu herkömmlichen Kunststoffen auf Rohölbasis. PHA Granula stellen mit ihrer komplexen Oberflächenstruktur aus diversen Proteinen kleine Funktionseinheiten (Organelle) dar, für die wir den Begriff „Carbonosomen“ geprägt haben.
In unserer AG untersuchen wir die an der subzellulären Bildung von PHB/PHA Granula beteiligten Proteine und deren individuellen Funktionen. Hierbei kommen insbesondere molekularbiologische Methoden und lifeimaging Techniken zum Einsatz (ii) Polyphosphat (PolyP) ist ein anorganisches Biopolymer, welches in allen Organismen vorkommt und daher von fundamentaler Bedeutung ist. In Bakterien untersuchen wir die Bildung und die spezifischen Funktionen von PolyP Granula mit molekularbiologische Methoden und lifeimagingTechniken. (iii) Polyisopren (Kautschuk, Gummi). Hier steht die Frage im Vordergrund, wie Gummi (Autoreifen!) von mikrobiellen Enzymen angegriffen und letztendlich abgebaut (mineralisiert) wird.
In den letzten Jahren haben wir eine neuartige Häm-haltige Dioxygenase (Rubberoxygenase RoxA) entdeckt und kürzlich deren Struktur aufgeklärt. Gegenwärtig untersuchen wir den oxidativen Reaktionsmechanismus mit biochemischen, biophysikalischen und molekularbiologischen Methoden.
Publikationen
Artikel:
Handrick, R., Reinhard, S. Jendrossek, D. 2000.
Mobilization of poly(3-hydroxybutyrate) in Ralstonia eutropha.
J. Bacteriol., 182:5916-5918
Jendrossek, D., R. Handrick. 2002.
Microbial degradation of polyhydroxyalkanoates.
Annu. Rev. Microbiol. 56:403-432
Handrick, R., Technow, U., Reichart, T., Reinhardt, S., Sander, T., Jendrossek, D. 2004.
The activator of the Rhodospirillum rubrum PHB depolymerase is a polypeptide that is extremely resistant to high temperature (121°C) and other physical or chemical stresses.
FEMS Microbiol. Lett., 230:265-74
Handrick, R., Reinhardt, S., Schultheiss, D., Reichart, T., D. Schüler, V. Jendrossek, D., Jendrossek, D. 2004.
Unraveling of the function of the Rhodospirillum rubrum activator of polyhydroxybutyrate (PHB) degradation: the activator is a PHB granule bound protein (phasin).
J. Bacteriol. 186:2466-75
Handrick, R., Reinhardt, S., Kimmig, P., Jendrossek, D. 2004.
The “intracellular” PHB depolymerase of Rhodospirillum rubrum is an periplasm-located enzyme with similarity to extracellular PHB depolymerases.
J. Bacteriol. 186:7243-7253
Gebauer, B., Jendrossek, D. 2006.
Assay of PHB Depolymerase activity and product determination.
Appl. Environ. Microbiol. 72:6094-6100
Jendrossek D., Selchow O., Hoppert M. 2007.
PHB granules at the early stages of formation are localized close to the cytoplasmic membrane in Caryophanon latum.
Appl Environ Microbiol. 73:586-593.
Hermawan, S. Jendrossek, D. 2007.
Microscopical investigation of PHB granules formation in Azotobacter vinelandii.
FEMS Microbiol. Lett. 266:60-64
Jendrossek. D. 2007.
Peculiarities of PHB granules preparation and PHA depolymerase activity determination.
Appl. Microbiol. Biotechnol. 74:1186-1196
Wang, L., Armbruster, W., Jendrossek, D. 2007.
Production of medium-chain length hydroxyalkanoic acids by pH stat.
Appl. Microbiol. Biotechnol. 74:1047-1053.
Uchino, K., Saito, B., Gebauer, B., Jendrossek, D. 2007.
Isolated Poly(3-hydroxybutyrate) (PHB) granules are complex bacterial organelles catalyzing formation of PHB from acetyl-CoA and degradation of PHB to acetyl-CoA.
J. Bacteriol. 189:8250-8256.
Uchino, K., Saito, T., Jendrossek, D. 2008
Poly(3-hydroxybutyrate) (PHB) depolymerase PhaZa1 is involved in mobilization of accumulated PHB in Ralstonia eutropha H16,
Appl Environ Microbiol. 74: 1058-1063.
Sznajder, A., Jendrossek, D. 2011.
Biochemical characterization of a new type of intracellular PHB depolymerase from Rhodospirillum rubrum with high hydrolytic activity on native PHB granules
Appl Microbiol Biotechnol 89:1487–1495
Cao C, Yudin Y, Bikard Y, Chen W, Liu T, Li H, Jendrossek D, Cohen A, Pavlov E, Rohacs T, Zakharian E (2013) Polyester modification of the mammalian TRPM8 channel protein: implications for structure and function. Cell Rep 4:302–315. doi: 10.1016/j.celrep.2013.06.022
Sznajder A, Jendrossek D (2014) To be or not to be a poly(3-hydroxybutyrate) (PHB) depolymerase: PhaZd1 (PhaZ6) and PhaZd2 (PhaZ7) of Ralstonia eutropha, highly active PHB depolymerases with no detectable role in mobilization of accumulated PHB. Appl Environ Microbiol 80:4936–4946. doi: 10.1128/AEM.01056-14
Tumlirsch T, Sznajder A, Jendrossek D (2015) Formation of polyphosphate by polyphosphate kinases and its relationship to poly(3-hydroxybutyrate) accumulation in Ralstonia eutropha strain H16. Appl Environ Microbiol 81:8277–8293. doi: 10.1128/AEM.02279-15
Quelas JI, Mesa S, Mongiardini EJ, Jendrossek D, Lodeiro AR (2016) Regulation of Polyhydroxybutyrate Synthesis in the Soil Bacterium Bradyrhizobium diazoefficiens. Appl Environ Microbiol 82:4299–4308. doi: 10.1128/AEM.00757-16
Klotz A, Georg J, Bučinská L, Watanabe S, Reimann V, Januszewski W, Sobotka R, Jendrossek D, Hess WR, Forchhammer K (2016) Awakening of a Dormant Cyanobacterium from Nitrogen Chlorosis Reveals a Genetically Determined Program. Current Biology 26:2862–2872. doi: 10.1016/j.cub.2016.08.054
Nowroth V, Marquart L, Jendrossek D (2016) Low temperature-induced viable but not culturable state of Ralstonia eutropha and its relationship to accumulated polyhydroxybutyrate. FEMS Microbiol Lett 363:fnw249. doi: 10.1093/femsle/fnw249
Kellici TF, Mavromoustakos T, Jendrossek D, Papageorgiou AC (2017) Crystal structure analysis, covalent docking and molecular dynamics calculations reveal a conformational switch in PhaZ7 PHB depolymerase. Proteins 276:36215. doi: 10.1002/prot.25296
Juengert J, Bresan S, Jendrossek D (2018) Determination of Polyhydroxybutyrate (PHB) Content in Ralstonia eutropha Using Gas Chromatography and Nile Red Staining. Bio-protocol. doi: 10.21769/BioProtoc.2748
Jüngert JR, Borisova M, Mayer C, Wolz C, Brigham CJ, Sinskey AJ, Jendrossek D (2017) Absence of ppGpp Leads to Increased Mobilization of Intermediately Accumulated Poly(3-hydroxybutyrate) (PHB) in Ralstonia eutropha H16. Appl Environ Microbiol AEM.00755–17. doi: 10.1128/AEM.00755-17
Adaya L, Millán M, Peña C, Jendrossek D, Espín G, Tinoco-Valencia R, Guzmán J, Pfeiffer D, Segura D (2018) Inactivation of an intracellular poly-3-hydroxybutyrate depolymerase of Azotobacter vinelandii allows to obtain a polymer of uniform high molecular mass. Appl Microbiol Biotechnol 187:6982–15. doi: 10.1007/s00253-018-8806-y
Jüngert JR, Patterson C, Jendrossek D (2018) Ralstonia eutropha's Poly(3-hydroxybutyrate)(PHB) polymerase PhaC1 and PHB depolymerase PhaZa1 are phosphorylated in vivo. Appl Environ Microbiol AEM.00604–18. doi: 10.1128/AEM.00604-18
Müller-Santos M, Koskimäki JJ, Alves LPS, de Souza EM, Jendrossek D, Pirttilä AM (2020) The protective role of PHB and its degradation products against stress situations in bacteria. FEMS Microbiol Rev 102:2693. doi: 10.1093/femsre/fuaa058
Artikel (Auswahl):
Jendrossek, D., Knoke, I., Habibian, R.B., Steinbüchel, A., Schlegel, H. G. 1993.
Degradation of poly(3-hydroxybutyrate), PHB, by bacteria and purification of a novel PHB depolymerase from Comamonas sp.
J. Environ. Polym. Degrad. 1:53-63.
Schirmer, A., Jendrossek, D., Schlegel, H. G. 1993.
Degradation of poly(3-hydroxyoctanoic acid) [P(3HO)] by bacteria: purification and properties of a P(3HO) depolymerase from Pseudomonas fluorescens GK13.
Appl. Environ. Microbiol. 59:1220-1227.
Schirmer, A., Jendrossek, D. 1994.
Molecular characterization of the extracellular poly(3-hydroxyoctanoic acid) [P(3HO)] depolymerase gene of Pseudomonas fluorescens GK13 and of its gene product.
J. Bacteriol. 176:7065-7073
Jendrossek, D., Frisse, A., Behrendes, A., Andermann, M., Kratzin, H. D., Stanislawski T., Schlegel, H. G. 1995.
Biochemical and molecular characterization of the Pseudomonas lemoignei polyhydroxyalkanoate (PHA) depolymerase system.
J. Bacteriol. 177:596-607
Behrends, A., Klingbeil, B., Jendrossek, D. 1996.
Poly(3-hydroxybutyrate) depolymerases bind to their substrate by a C-terminal located substrate binding site.
FEMS Microbiol. Lett. 143:191-194.
Molitoris, K. P., Moss, S. T., de Koning, G. Jendrossek, D. 1996.
SEM analysis of poly-hydroxyalkanoate degradation by bacteria.
Appl. Microbiol. Biotechnol. 46:570-579.
Jendrossek, D. Schirmer, A., Schlegel, H. G. 1996.
Biodegradation of polyhydroxyalkanoic acids, Review,
Appl. Microbiol. Biotechnol. 46:451-463.
Jendrossek, D., Schirmer, A., Handrick, R. 1997.
Recent advances in characterization of bacterial PHA depolymerases.
In : Eggink, G., Steinbüchel, A., Poirier, Y., Witholt, B. (Eds.). 1996 International Symposium on bacterial polyhydroxyalkanoates. NRC Research Press, Ottawa, Canada.
Spyros, A, Kimmrich, Briese, B.H., Jendrossek, D. 1997.
1H-NMR imaging study of enzymatic degradation in poly(3-hydroxybutyrate) and poly(3-hydroxybutyrate-co-3-hydroxyvalerate). Evidence for preferential degradation of the amorphous phase by the depolymerase B from Pseudomonas lemoignei.
Macromolecules 30:8218-8225.
Terpe, K., Kerkhoff, K., Pluta, E. Jendrossek, D 1999.
Relationship between succinate transport and production of extracellular poly(3-hydroxybutyrate) depolymerase in Pseudomonas lemoignei.
Appl. Environm. Microbiol. 65:1703-1709.
Focarete, M.L., Scandola, M., Jendrossek, D., Adamus, G. Sikorska, W. Kowalczuk, M. 1999.
Bioassimilation of oligomers of atactic poly[(R,S)-3-hydroxybutyrate] by selected bacterial strains.
Macromolecules 32:4814-4818.
Jendrossek, D. 2001.
Transfer of [Pseudomanas] lemoignei, a Gram-negative rod with restricted catabolic capacity, to Paucimonas gen. nov. with one species, Paucimonas lemoignei comb. nov.
Int. J. Syst. Evol. Microbiol. 51:905-908
Handrick, R., Reinhardt, S., Focarete, M.L., Scandola, M., Adamus, G., Kowalczuk, M., Jendrossek, D. 2001.
A new type of thermoalkalophilic hydrolase of Paucimonas lemoignei with high specificity for amorphous polyesters of short-chain-length hydroxyalkanoic acids.
J. Biol. Chem., 276:36215-36224.
Reinhardt, S., Handrick, R., Jendrossek, D. 2002.
The „PHB depolymerase inhibitor“ of Paucimonas lemoignei is a PHB depolymerase.
Biomacromolecules 3:823-827.
Jendrossek, D., R. Handrick. 2002.
Microbial degradation of polyhydroxyalkanoates.
Annu. Rev. Microbiol. 56:403-432
Elbanna, K., Lütke-Eversloh, T., Jendrossek, D., Steinbüchel, A. 2004.
Studies on the biodegradability of polythioesters by polyhydroxyalkanoate (PHA) degrading bacteria and PHA depolymerases.
Arch. Microbiol. 182:212-225
Kapetaniou EG, Braaz R, Jendrossek D., Papageorgiou AC. 2005.
Crystallization and preliminary X-ray analysis of a novel thermoalkalophilic poly(3-hydroxybutyrate) depolymerase (PhaZ7) from Paucimonas lemoignei.
Acta Crystallograph Sect F Struct Biol Cryst Commun. 61:479-81.
Gebauer, B., Jendrossek, D. 2006.
Assay of PHB Depolymerase activity and product determination.
Appl. Environ. Microbiol. 72:6094-6100
Jendrossek. D. 2007.
Peculiarities of PHB granules preparation and PHA depolymerase activity determination.
Appl. Microbiol. Biotechnol. 74:1186-1196
Papageorgiou, A.C., Hermawan, S., Singh, C.B., and Jendrossek, D. 2008.
Structural basis of poly(3-hydroxybutyrate) hydrolysis by PhaZ7 depolymerase from Paucimonas lemoignei.
J Mol Biol 382: 1184-1194.
Hermawan S., Jendrossek D. 2010.
Tyrosine 105 of Paucimonas lemoignei PHB depolymerase PhaZ7 is essential for polymer binding.
Polymer Degradation and Stability 95: 1429-1435
Wakadkar, S., Hermawan, S., Jendrossek, D., Papageorgiou, A.C. 2010.
The structure of PhaZ7 at atomic (1.2 °A) resolution reveals details of the active site and suggests a substrate-binding mode. Acta Cryst. F66, 648–654
Jendrossek D, Hermawan S, Subedi B, Papageorgiou AC (2013) Biochemical analysis and structure determination of Paucimonas lemoignei poly(3-hydroxybutyrate) (PHB) depolymerase PhaZ7 muteins reveal the PHB binding site and details of substrate-enzyme interactions. Mol Microbiol 90:649–664. doi: 10.1111/mmi.12391
Artikel:
Jendrossek D. 2005. Fluorescence microscopical investigation of poly(3-hydroxybutyrate) granule formation in bacteria. Biomacromolecules, 10.1021/bm049441r
Hermawan S, Jendrossek D. 2006. Microscopical investigation of poly(3-hydroxybutyrate) granule formation in Azotobacter vinelandii. FEMS Microbiol Lett DOI:10.1111/j.1574-6968.2006.00506.x
Jendrossek D. Selchow O, Hoppert M. 2007. Poly(3-Hydroxybutyrate) granules at the early stages of formation are localized close to the cytoplasmic membrane in Caryophanon latum, Appl Environ Microbiol 77: 586–593, doi:10.1128/AEM.01839-06
Jendrossek D. 2009. Polyhydroxyalkanoate granules are complex subcellular organelles (Carbonosomes. J Bacteriol 191. doi:10.1128/JB.01723-08
Pfeiffer D, Wahl A, Jendrossek D. 2011. Identification of a multifunctional protein, PhaM, that determines number, surface to volume ratio, subcellular localization and distribution to daughter cells of poly(3-hydroxybutyrate), PHB, granules in Ralstonia eutropha H16. Mol Microbiol 82:936–951.
Pfeiffer D, Jendrossek D. 2011. Interaction between poly(3-hydroxybutyrate) granule-associated proteins as revealed by two-hybrid analysis and identification of a new phasin in Ralstonia eutropha H16. Microbiology 157:2795–2807.
Pfeiffer D, Jendrossek D. 2012. Localization of poly(3-hydroxybutyrate) (PHB) granule-associated proteins during PHB granule formation and identification of two new phasins, PhaP6 and PhaP7, in Ralstonia eutropha H16. J Bacteriol 194:5909–5921.
Wahl A, Schuth N, Pfeiffer D, Nussberger S, Jendrossek D. 2012. PHB granules are attached to the nucleoid via PhaM in Ralstonia eutropha. BMC Microbiol 12:262.
Jendrossek D, Pfeiffer D. 2014. New insights in the formation of polyhydroxyalkanoate granules (carbonosomes) and novel functions of poly(3-hydroxybutyrate). Environ Microbiol 16:2357–2373.
Pfeiffer D, Jendrossek D. 2014. PhaM is the physiological activator of poly(3-hydroxybutyrate) (PHB) synthase (PhaC1) in Ralstonia eutropha. Appl Environ Microbiol 80:555–563.
Sznajder A, Jendrossek D. 2014. To be or not to be a PHB depolymerase: PhaZd1 (PhaZ6) and PhaZd2 (PhaZ7) of Ralstonia eutropha are highly active PHB depolymerases but have no detectable role in mobilization of accumulated PHB. Appl Environ Microbiol 16:4936–4946.
Tumlirsch T, Sznajder A, Jendrossek D. 2015. Formation of polyphosphate by polyphosphate kinases and its relationship to PHB accumulation in Ralstonia eutropha H16. Appl Environ Microbiol 81:8277–8293.
Bresan S, Sznajder A, Hauf W, Forchhammer K, Pfeiffer D, Jendrossek D. 2016. Polyhydroxyalkanoate (PHA) granules have no phospholipids. Sci Rep 6:26612.
Bresan S, Jendrossek D. 2017. New insights into PhaM-PhaC-mediated localization of polyhydroxybutyrate granules in Ralstonia eutropha H16. Appl Environ Microbiol 83:e00505-17. https://doi.org/10.1128/AEM
Jüngert, J. R., Patterson, C., & Jendrossek, D. 2018. Ralstonia eutropha's Poly(3-hydroxybutyrate)(PHB) polymerase PhaC1 and PHB depolymerase PhaZa1 are phosphorylated in vivo. Appl Environ Microbiol AEM 84:e00604, doi.org/10.1128/AEM.00604-18
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