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  1. Book ; Online ; E-Book: Bacterial organelles and organelle-like inclusions

    Jendrossek, Dieter

    (Microbiology monographs ; Volume 34)

    2020  

    Abstract: The authors of this contributed volume define various inclusions and supramolecular structures in prokaryotes as discrete bodies. Research on the biosynthesis, reutilization and physiological functions of the accumulated structures is still in progress, ... ...

    Author's details Dieter Jendrossek
    Series title Microbiology monographs ; Volume 34
    Abstract The authors of this contributed volume define various inclusions and supramolecular structures in prokaryotes as discrete bodies. Research on the biosynthesis, reutilization and physiological functions of the accumulated structures is still in progress, while the interest in these inclusions is still growing. Within this second edition, the new editor organized updates to the most important contributions of the original volume. The chapters discuss the most prominent inclusion examples such as gas vesicles, inorganic inclusions (sulfur globules, magnetosomes, polyphosphatosomes), carbon-based inclusions (lipid bodies, carbonosomes, granulose, cyanophycin) as well as other organelle-like microcompartments (carboxysomes, anammoxosomes), thus making this volume a fascinating read for scientists with a keen interest in microbiology.
    Keywords Plant organelles
    Subject code 571.6592
    Language English
    Size 1 online resource (VII, 275 p. 42 illus., 29 illus. in color.)
    Edition Second edition.
    Publisher Springer
    Publishing place Cham, Switzerland
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 3-030-60173-0 ; 3-030-60172-2 ; 978-3-030-60173-7 ; 978-3-030-60172-0
    DOI 10.1007/978-3-030-60173-7
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Article ; Online: Cleavage of natural rubber by rubber oxygenases in Gram-negative bacteria.

    Prakash, Tulika / Yadav, Sandhya R / Bürger, Marius / Jendrossek, Dieter

    Applied microbiology and biotechnology

    2024  Volume 108, Issue 1, Page(s) 191

    Abstract: Bacterial degradation of natural rubber (NR) in an oxic environment is initiated by oxidative cleavage of double bonds in the NR-carbon backbone and is catalyzed by extracellular haem-containing rubber oxygenases. NR-cleavage products of sufficiently low ...

    Abstract Bacterial degradation of natural rubber (NR) in an oxic environment is initiated by oxidative cleavage of double bonds in the NR-carbon backbone and is catalyzed by extracellular haem-containing rubber oxygenases. NR-cleavage products of sufficiently low molecular mass are taken up by the cells and metabolized for energy and biomass formation. Gram-negative and Gram-positive NR-degrading bacteria (usually) employ different types of rubber oxygenases such as RoxA and/or RoxB (most Gram-negative NR-degraders) or latex clearing protein Lcp (most Gram-positive NR-degraders). In order to find novel orthologues of Rox proteins, we have revisited databases and provide an update of Rox-like proteins. We describe the putative evolution of rubber oxygenases and confirm the presence of a third subgroup of Rox-related proteins (RoxCs), the biological function of which remains, however, unclear. We summarize the knowledge on the taxonomic position of Steroidobacter cummioxidans 35Y and related species. Comparison of genomic and biochemical features of strain 35Y with other species of the genus Steroidobacter suggests that strain 35Y represents a species of a novel genus for which the designation Aurantibaculum gen. nov. is proposed. A short summary on the capabilities of NR-degrading consortia, that could be superior in biotechnological applications compared to pure cultures, is also provided. KEY POINTS: • Three types of rubber oxygenases exist predominantly in Gram-negative microbes • S. cummioxidans 35Y contains RoxA and RoxB which are superior in activity • S. cummioxidans 35Y represents a species of a novel genus.
    MeSH term(s) Rubber/metabolism ; Oxygenases/metabolism ; Bacterial Proteins/metabolism ; Latex/metabolism ; Gram-Negative Bacteria/genetics ; Gram-Negative Bacteria/metabolism
    Chemical Substances Rubber (9006-04-6) ; Oxygenases (EC 1.13.-) ; Bacterial Proteins ; Latex
    Language English
    Publishing date 2024-02-02
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-023-12940-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  3. Article ; Online: Acidocalcisomes and Polyphosphate Granules Are Different Subcellular Structures in Agrobacterium tumefaciens.

    Frank, Celina / Jendrossek, Dieter

    Applied and environmental microbiology

    2020  Volume 86, Issue 8

    Abstract: Acidocalcisomes are membrane-enclosed, polyphosphate-containing acidic organelles in ... ...

    Abstract Acidocalcisomes are membrane-enclosed, polyphosphate-containing acidic organelles in lower
    MeSH term(s) Agrobacterium tumefaciens/physiology ; Microscopy, Fluorescence ; Organelles/metabolism ; Polyphosphates/metabolism
    Chemical Substances Polyphosphates
    Language English
    Publishing date 2020-04-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/AEM.02759-19
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Migration of Polyphosphate Granules in Agrobacterium tumefaciens.

    Frank, Celina / Pfeiffer, Daniel / Aktas, Meriyem / Jendrossek, Dieter

    Microbial physiology

    2022  Volume 32, Issue 3-4, Page(s) 71–82

    Abstract: Agrobacterium tumefaciens has two polyphosphate (polyP) kinases, one of which (PPK1AT) is responsible for the formation of polyP granules, while the other (PPK2AT) is used for replenishing the NTP pools by using polyP as a phosphate donor to ... ...

    Abstract Agrobacterium tumefaciens has two polyphosphate (polyP) kinases, one of which (PPK1AT) is responsible for the formation of polyP granules, while the other (PPK2AT) is used for replenishing the NTP pools by using polyP as a phosphate donor to phosphorylate nucleoside diphosphates. Fusions of eYFP with PPK2AT or of the polyP granule-associated phosin PptA from Ralstonia eutropha always co-localized with polyP granules in A. tumefaciens and allowed the tracking of polyP granules in time-lapse microscopy experiments without the necessity to label the cells with the toxic dye DAPI. Fusions of PPK1AT with mCherry formed fluorescent signals often attached to, but not completely co-localizing with, polyP granules in wild-type cells. Time-lapse microscopy revealed that polyP granules in about one-third of a cell population migrated from the old pole to the new cell pole shortly before or during cell division. Many cells de novo formed a second (nonmigrating) polyP granule at the opposite cell pole before cell division was completed, resulting in two daughter cells each having a polyP granule at the old pole after septum formation. Migration of polyP granules was disordered in mitomycin C-treated or in PopZ-depleted cells, suggesting that polyP granules can associate with DNA or with other molecules that are segregated during the cell cycle.
    MeSH term(s) Agrobacterium tumefaciens/genetics ; Bacterial Proteins/genetics ; Cell Division ; Cupriavidus necator/genetics ; Polyphosphates/metabolism
    Chemical Substances Bacterial Proteins ; Polyphosphates
    Language English
    Publishing date 2022-02-15
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3042601-7
    ISSN 2673-1673 ; 2673-1665
    ISSN (online) 2673-1673
    ISSN 2673-1665
    DOI 10.1159/000521970
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: The Multiple Roles of Polyphosphate in Ralstonia eutropha and Other Bacteria.

    Rosigkeit, Hanna / Kneißle, Lea / Obruča, Stanislav / Jendrossek, Dieter

    Microbial physiology

    2021  Volume 31, Issue 2, Page(s) 163–177

    Abstract: An astonishing variety of functions has been attributed to polyphosphate (polyP) in prokaryotes. Besides being a reservoir of phosphorus, functions in exopolysaccharide formation, motility, virulence and in surviving various forms of stresses such as ... ...

    Abstract An astonishing variety of functions has been attributed to polyphosphate (polyP) in prokaryotes. Besides being a reservoir of phosphorus, functions in exopolysaccharide formation, motility, virulence and in surviving various forms of stresses such as exposure to heat, extreme pH, oxidative agents, high osmolarity, heavy metals and others have been ascribed to polyP. In this contribution, we will provide a historical overview on polyP, will then describe the key proteins of polyP synthesis, the polyP kinases, before we will critically assess of the underlying data on the multiple functions of polyP and provide evidence that - with the exception of a P-storage-function - most other functions of polyP are not relevant for survival of Ralstonia eutropha, a biotechnologically important beta-proteobacterial species.
    MeSH term(s) Cupriavidus necator ; Polyphosphates
    Chemical Substances Polyphosphates
    Language English
    Publishing date 2021-05-20
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 3042601-7
    ISSN 2673-1673 ; 2673-1665
    ISSN (online) 2673-1673
    ISSN 2673-1665
    DOI 10.1159/000515741
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Solimonas fluminis has an active latex-clearing protein.

    Birke, Jakob / Jendrossek, Dieter

    Applied microbiology and biotechnology

    2019  Volume 103, Issue 19, Page(s) 8229–8239

    Abstract: The utilization of rubber (poly (cis-1,4-isoprene)) by rubber-degrading bacteria depends on the synthesis of rubber oxygenases that cleave the polymer extracellularly to low molecular weight products that can be taken up and used as a carbon source. All ... ...

    Abstract The utilization of rubber (poly (cis-1,4-isoprene)) by rubber-degrading bacteria depends on the synthesis of rubber oxygenases that cleave the polymer extracellularly to low molecular weight products that can be taken up and used as a carbon source. All so far described Gram-negative rubber-degrading species use two related ≈ 70 kDa rubber oxygenases (RoxA and RoxB) for the primary attack of rubber while all described Gram-positive rubber-degrading strains use RoxA/RoxB-unrelated latex-clearing proteins (Lcps, ≈ 40 kDa) as rubber oxygenase(s). In this study, we identified an lcp orthologue in a Gram-negative species (Solimonas fluminis). We cloned and heterologously expressed the lcp gene of S. fluminis HR-BB, purified the corresponding Lcp protein (Lcp
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/isolation & purification ; Bacterial Proteins/metabolism ; Biotransformation ; Cloning, Molecular ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gammaproteobacteria/enzymology ; Gammaproteobacteria/genetics ; Gene Expression ; Latex/metabolism ; Oxygenases/genetics ; Oxygenases/isolation & purification ; Oxygenases/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism
    Chemical Substances Bacterial Proteins ; Latex ; Recombinant Proteins ; Oxygenases (EC 1.13.-)
    Language English
    Publishing date 2019-09-04
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-019-10085-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Characterization of Agrobacterium tumefaciens PPKs reveals the formation of oligophosphorylated products up to nucleoside nona-phosphates.

    Frank, Celina / Teleki, Attila / Jendrossek, Dieter

    Applied microbiology and biotechnology

    2020  Volume 104, Issue 22, Page(s) 9683–9692

    Abstract: Agrobacterium tumefaciens synthesizes polyphosphate (polyP) in the form of one or two polyP granules per cell during growth. The A. tumefaciens genome codes for two polyphosphate kinase genes, ... ...

    Abstract Agrobacterium tumefaciens synthesizes polyphosphate (polyP) in the form of one or two polyP granules per cell during growth. The A. tumefaciens genome codes for two polyphosphate kinase genes, ppk1
    MeSH term(s) Adenine Nucleotides ; Agrobacterium tumefaciens/genetics ; Nucleosides ; Nucleotides ; Polyphosphates
    Chemical Substances Adenine Nucleotides ; Nucleosides ; Nucleotides ; Polyphosphates
    Language English
    Publishing date 2020-10-06
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-020-10891-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Book ; Online ; Thesis: Funktionale und strukturelle Charakterisierung von Polyphosphat und Polyphosphat-assoziierten Proteinen im ß-Proteobakterium Ralstonia eutropha H16

    Rosigkeit, Hanna [Verfasser] / Jendrossek, Dieter [Akademischer Betreuer]

    2022  

    Author's details Hanna Rosigkeit ; Betreuer: Dieter Jendrossek
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language German
    Publisher Universitätsbibliothek der Universität Stuttgart
    Publishing place Stuttgart
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  9. Article: Rubber oxygenases

    Jendrossek, Dieter / Birke, Jakob

    Applied microbiology and biotechnology. 2019 Jan., v. 103, no. 1

    2019  

    Abstract: Natural rubber (NR), poly(cis-1,4-isoprene), is used in an industrial scale for more than 100 years. Most of the NR-derived materials are released to the environment as waste or by abrasion of small particles from our tires. Furthermore, compounds with ... ...

    Abstract Natural rubber (NR), poly(cis-1,4-isoprene), is used in an industrial scale for more than 100 years. Most of the NR-derived materials are released to the environment as waste or by abrasion of small particles from our tires. Furthermore, compounds with isoprene units in their molecular structures are part of many biomolecules such as terpenoids and carotenoids. Therefore, it is not surprising that NR-degrading bacteria are widespread in nature. NR has one carbon-carbon double bond per isoprene unit and this functional group is the primary target of NR-cleaving enzymes, so-called rubber oxygenases. Rubber oxygenases are secreted by rubber-degrading bacteria to initiate the break-down of the polymer and to use the generated cleavage products as a carbon source. Three main types of rubber oxygenases have been described so far. One is rubber oxygenase RoxA that was first isolated from Xanthomonas sp. 35Y but was later also identified in other Gram-negative rubber-degrading species. The second type of rubber oxygenase is the latex clearing protein (Lcp) that has been regularly found in Gram-positive rubber degraders. Recently, a third type of rubber oxygenase (RoxB) with distant relationship to RoxAs was identified in Gram-negative bacteria. All rubber oxygenases described so far are haem-containing enzymes and oxidatively cleave polyisoprene to low molecular weight oligoisoprenoids with terminal CHO and CO–CH3 functions between a variable number of intact isoprene units, depending on the type of rubber oxygenase. This contribution summarises the properties of RoxAs, RoxBs and Lcps.
    Keywords Gram-negative bacteria ; Xanthomonas ; carbon ; carotenoids ; chemical bonding ; cleavage (chemistry) ; isoprene ; latex ; moieties ; molecular weight ; oxygenases ; polymers ; rubber ; tires ; wastes
    Language English
    Dates of publication 2019-01
    Size p. 125-142.
    Publishing place Springer Berlin Heidelberg
    Document type Article
    Note Review
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-018-9453-z
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

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  10. Article ; Online: New Insights into PhaM-PhaC-Mediated Localization of Polyhydroxybutyrate Granules in Ralstonia eutropha H16.

    Bresan, Stephanie / Jendrossek, Dieter

    Applied and environmental microbiology

    2017  Volume 83, Issue 12

    Abstract: The formation and localization of polyhydroxybutyrate (PHB) granules ... ...

    Abstract The formation and localization of polyhydroxybutyrate (PHB) granules in
    Language English
    Publishing date 2017-06-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 223011-2
    ISSN 1098-5336 ; 0099-2240
    ISSN (online) 1098-5336
    ISSN 0099-2240
    DOI 10.1128/AEM.00505-17
    Database MEDical Literature Analysis and Retrieval System OnLINE

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