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  • 1
    Online Resource
    Online Resource
    Bacterial Organelles and Organelle-like Inclusions (2020)
    Cham :Springer International Publishing :
    Details
    Keywords: Microbiology. ; Bacteria. ; Lipids. ; Proteins . ; Microbiology. ; Bacteria. ; Lipidology. ; Protein Biochemistry.
    Description / Table of Contents: Polyphosphate Granules and Acidocalcisomes -- Bacterial Intracellular Sulphur Globules -- Biosynthesis and Intracellular Organization of Magnetosomes in Magnetotactic Bacteria -- Gas Vesicles of Archaea and Bacteria -- The Anammoxosome Organelle: The Power Plant of Anaerobic Ammonium-Oxidizing (anammox) Bacteria -- Bacterial Microcompartments -- The Cyanophycin Granule Peptide from Cyanobacteria -- Storage Polysaccharides in Prokaryotes: Glycogen, Granulose and Starch-like Granules -- Wax Ester and Triacylglycerol Inclusions -- Carbonosomes.
    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.
    Type of Medium: Online Resource
    Pages: VII, 275 p. 42 illus., 29 illus. in color. , online resource.
    Edition: 2nd ed. 2020.
    ISBN: 9783030601737
    Series Statement: Microbiology Monographs, 34
    URL: https://doi.org/10.1007/978-3-030-60173-7
    DOI: 10.1007/978-3-030-60173-7
    DDC: 579
    Language: English
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  • 2
    Electronic Resource
    Electronic Resource
    Identification and characterisation of the catalytic triad of the alkaliphilic thermotolerant PHA depolymerase PhaZ7 of Paucimonas lemoignei (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 224 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The recently discovered extracellular poly[(R)-3-hydroxybutyrate] (PHB) depolymerase PhaZ7 of Paucimonas lemoignei represents the first member of a new subgroup (EC 3.1.1.75) of serine hydrolases with no significant amino acid similarities to conventional PHB depolymerases, lipases or other hydrolases except for a potential lipase box-like motif (Ala-His-Ser136-Met-Gly) and potential candidates for catalytic triad and oxyanion pocket amino acids. In order to identify amino acids essential for activity 11 mutants of phaZ7 were generated by site-directed mutagenesis and expressed in recombinant protease-deficient Bacillus subtilis WB800. The wild-type depolymerase and 10 of the 11 mutant proteins (except for Ser136Cys) were expressed and efficiently secreted by B. subtilis as shown by Western blots of cell-free culture fluid proteins. No PHB depolymerase activity was detected in strains harbouring one of the following substitutions: His47Ala, Ser136Ala, Asp242Ala, Asp242Asn, His306Ala, indicating the importance of these amino acids for activity. Replacement of Ser136 by Thr resulted in a decrease of activity to about 20% of the wild-type level and suggested that the hydroxy group of the serine side chain is important for activity but can be partially replaced by the hydroxy function of threonine. Alterations of Asp256 to Ala or Asn or of the putative serine hydrolase pentapeptide motif (Ala-His-Ser136-Met-Gly) to a lipase box consensus sequence (Gly134-His-Ser136-Met-Gly) or to the PHB depolymerase box consensus sequence (Gly134-Leu135-Ser136-Met-Gly) had no significant effect on PHB depolymerase activity, indicating that these amino acids or sequence motifs were not essential for activity. In conclusion, the PHB depolymerase PhaZ7 is a serine hydrolase with a catalytic triad and oxyanion pocket consisting of His47, Ser136, Asp242 and His306.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00425-7
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  • 3
    Electronic Resource
    Electronic Resource
    Sequence analysis of a gene product synthesized by Xanthomonas sp. during growth on natural rubber latex (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 224 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Xanthomonas sp. secretes an extracellular protein (Mr∼70±5 kDa) during growth on purified natural rubber [poly(1,4-cis-isoprene)] but not during growth on water-soluble carbon sources such as glucose or gluconate. A 1.3 kbp DNA fragment coding for an internal part of the structural gene of the 70 kDa protein was amplified by nested polymerase chain reaction (PCR) using amino acid sequence information obtained after Edman degradation of selected trypsin-generated peptides of the purified 70 kDa protein. The PCR product was used as a DNA probe to clone the complete structural gene from genomic DNA of Xanthomonas sp. The sequenced DNA contained a 2037 bp open reading frame which coded for a polypeptide of 678 amino acids (Mr 74.6 kDa) and which included the features of the N-terminal signal peptidase cleavage site (Mr∼72.9 kDa for the mature protein). Analysis of the amino acid sequence revealed the presence of two heme binding motifs (CXXCH) and a ∼20 amino acids long sequence that is conserved in the Paracoccus denitrificans and Pseudomonas aeruginosa diheme cytochrome c peroxidases (CCPs). This region includes a histidine residue (H519 in Xanthomonas sp. and H265 and H271 in the Pseudomonas strains, respectively) that is essential for activity in CCPs and that is also conserved in other bacterial oxidases. Blast analysis confirmed the relatedness of the 70 kDa protein to heme-containing oxidases and suggested that it is a member of a new family of relatively large (∼500 to ∼1000 amino acids) extracellular proteins with so far unknown function being only far related in amino acid sequence to P. denitrificans and P. aeruginosa CCPs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00424-5
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  • 4
    Electronic Resource
    Electronic Resource
    MICROBIAL DEGRADATION OF POLYHYDROXYALKANOATES* (2002)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Microbiology 56 (2002), S. 403-432 
    Details
    ISSN: 0066-4227
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Notes: Abstract Polyesters such as poly(3-hydroxybutyrate) (PHB) or other polyhydroxyalkanoates (PHA) have attracted commercial and academic interest as new biodegradable materials. The ability to degrade PHA is widely distributed among bacteria and fungi and depends on the secretion of specific extracellular PHA depolymerases (e-PHA depolymerases), which are carboxyesterases (EC 3.1.1.75 and EC 3.1.1.76), and on the physical state of the polymer (amorphous or crystalline). This contribution provides a summary of the biochemical and molecular biological characteristics of e-PHA depolymerases and focuses on the intracellular mobilization of storage PHA by intracellular PHA depolymerases (i-PHA depolymerases) of PHA-accumulating bacteria. The importance of different assay systems for PHA depolymerase activity is also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.micro.56.012302.160838
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  • 5
    Electronic Resource
    Electronic Resource
    Bacterial degradation of natural rubber: a privilege of actinomycetes? (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 150 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Using natural rubber latex as the sole source of carbon and energy 50 rubber-degrading bacteria were isolated. Out of those 50 isolates, 33 were identified as Streptomyces species and 8 as Micromonospora species. Screening of 1220 bacteria obtained from different culture collections revealed 46 additional rubber-degrading bacteria (Streptomyces 31 strains, Micromonospora 5, Actinoplanes 3, Nocardia 2, Dactylosporangium 1, Actinomadura 1, unidentified 3). All rubber-degrading isolates were identified as members of the actinomycetes, a large group of mycelium-forming Gram-positive bacteria. Interestingly no Gram-negative bacterium could be isolated. In most strains expression of extracellular rubber-degrading enzymes was repressed by glucose and/or succinate. The reduction of the average molecular mass of solution-cast films of natural rubber from 640.000 to 25.000 in liquid culture upon bacterial growth indicates the participation of an endo-cleavage mechanism of degradation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10368.x
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  • 6
    Electronic Resource
    Electronic Resource
    Production of PHA depolymerase A (PhaZ5) from Paucimonas lemoignei in Bacillus subtilis (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 209 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Purification of poly(3-hydroxybutyrate) depolymerase (EC 3.1.1.75) from Paucimonas lemoignei is complicated because the bacterium produces several isoenzymes which are difficult to separate from each other. The phaZ5 gene of P. lemoignei encoding extracellular poly(3-hydroxybutyrate) depolymerase A was functionally expressed from the constitutive P43 promoter of pWB980 in a multiple protease-negative mutant of Bacillus subtilis (strain WB800) and secreted to the culture medium. The depolymerase (apparent Mr, 42 kDa; 1.9 mg purified protein per liter culture) was purified from cell-free culture fluid to homogenity by applying only one chromatography step in comparison to at least two necessary steps if poly(3-hydroxybutyrate) depolymerases are purified from P. lemoignei. The recombinant depolymerase lacked any carbohydrate content in contrast to the glycosylated depolymerase of the wild-type. Glycosylation was not essential for activity but enhanced the thermal stability of the enzyme at high temperature. Overexpression of poly(3-hydroxybutyrate) depolymerase in B. subtilis is more efficient than in Escherichia coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11137.x
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  • 7
    Electronic Resource
    Electronic Resource
    A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerases (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 167 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A fragment of genomic DNA from Sulfolobus acidocaldarius DSM 639 encoding a lipolytic enzyme was cloned and sequenced. The 314-amino acid polypeptide displays a maximum sequence similarity (43%) to a putative polyhydroxyalkanoate depolymerase from Pseudomonas oleovorans and contains the pentapeptide G-X1-S-X2-G which is typical of serine hydrolases. The protein is highly thermostable and is able to hydrolyse a variety of lipid substrates thus providing a promising tool for potential biotechnological applications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13209.x
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  • 8
    Electronic Resource
    Electronic Resource
    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 (2004)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 230 (2004), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Hydrolysis of native (amorphous) polyhydroxybutyrate (nPHB) granules isolated from different sources by soluble PHB depolymerase of Rhodospirillum rubrum in vitro requires the presence of a heat-stable compound (activator). The activator was purified and was resistant against various physical and chemical stresses such as heat (up to 130°C), pH 1–12, dryness, oxidation by H2O2, reducing and denaturing compounds (2-mercaptoethanol, 5 M guanidinium-HCl) and many solvents including phenol/chloroform. The activator coding gene was identified by N-terminal sequencing of the purified protein, and the deduced protein showed significant homology to magnetosome-associated protein (Mms16) of magnetotactic bacteria. Analysis of the activation process in vitro showed that the activator acts on nPHB granules but not on the depolymerase. The effect of the activator could be mimicked by pretreatment of nPHB granules with trypsin or other proteases but protease activity of the purified activator was not detected. Evidence is shown that different mechanisms were responsible for activation of nPHB by trypsin and activator, respectively. PHB granule-associated protein (PhaP) of Ralstonia eutropha nPHB granules were cleaved by trypsin but no cleavage occurred after activator treatment. Hydrolysis of artificial protein-free PHB granules coated with negatively charged detergents (sodium dodecyl sulfate (SDS), cholate but not cetyltrimethyl-ammonium bromide (CTAB)) did not require activation and confirmed that surface layer proteins of nPHB granules are the targets of the activator rather than lipids. All experimental data are in agreement with the assumption that trypsin and the activator enable the PHB depolymerase to find and to bind to the polymer surface: trypsin by removing a portion of proteins from the polymer surface, the activator by modifying the surface structure in a not yet understood manner presumably by interaction with phasins of the proteinous surface layer of nPHB.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00919-4
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  • 9
    Electronic Resource
    Electronic Resource
    Determination of the active sites serine of the poly (3-hydroxybutyrate) depolymerases of Pseudomonas lemoignei (PhaZ5) and of Alcaligenes faecalis (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 141 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Mutational analysis of the poly(3-hydroxybutyrate) (PHB) depolymerase A of Pseudomonas lemoignei and of the poly(3-hydroxybutyrate) depolymerase of Alcaligenes faecalis revealed that S138 (P. lemoignei) and S139 (A. faecalis) are essential for activity. Both serines are part of a strictly conserved pentapeptide sequence which is present in all poly(3-hydroxybutyrate) depolymerases analyzed so far (G-L-S-S(A)-G) and which resembles the lipase box of lipases and other serine hydrolases (G-X-S-X-G). Mutation of another conserved serine, namely S195 (P. lemoignei) and S196 (A. faecalis), resulted in mutant proteinswith almost full activity and proved that S195 and S196 are not essential for activity. The results indicate the structural and functional relationship of poly(3-hydroxybutyrate) depolymerases to the family of serine hydrolases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08370.x
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  • 10
    Electronic Resource
    Electronic Resource
    Malate:quinone oxidoreductase (MqoB) is required for growth on acetate and linear terpenes in Pseudomonas citronellolis (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 246 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Mini-transposon-induced mutants with defects in utilization of linear terpenes such as citronellol and citronellic acid were isolated from Pseudomonas citronellolis. Mutants with strongly reduced growth on citronellol and citronellic acid (class I) were obtained together with mutants growing normally on citronellic acid but with impairment in growth on citronellol (class II) and auxotroph mutants (class III). The transposon carrying DNA fragments of two class I mutants were cloned and malate:quinone oxidoreductase gene (mqoB) was identified as the transposon insertion site in both mutants. The mqoB genes of P. aeruginosa and of P. citronellolis wild types were cloned. Conjugative transfer of the mqoB genes to the two P. citronellolis mutants increased the strongly reduced levels of MqoB activity in cell extracts of the mutants to the level of the wild type and restored the ability of the mutants to grow on citronellol and citronellic acid. Physiological analysis of the wild type and of mutants showed that MqoB is part of the glyoxylate cycle in P. citronellolis and is necessary for growth on C2-compounds and linear terpenes such as citronellol or citronellic acid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2005.03.034
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