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  1. Book ; Online ; Thesis: Deg Proteases in Arabidopsis thaliana

    Schuhmann, Holger

    2008  

    Title variant Deg-Proteasen in Arabidopsis thaliana
    Author's details Holger Schuhmann
    Language English
    Size Online-Ressource
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss--Konstanz, 2008
    Database Library catalogue of the German National Library of Science and Technology (TIB), Hannover

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  2. Book ; Online ; Thesis: Deg Proteases in Arabidopsis thaliana

    Schuhmann, Holger

    2008  

    Title variant Deg-Proteasen in Arabidopsis thaliana
    Author's details Holger Schuhmann
    Language English
    Size Online-Ressource
    Document type Book ; Online ; Thesis
    Thesis / German Habilitation thesis Univ., Diss--Konstanz, 2008
    Database Former special subject collection: coastal and deep sea fishing

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  3. Article ; Online: Deg proteases and their role in protein quality control and processing in different subcellular compartments of the plant cell.

    Schuhmann, Holger / Adamska, Iwona

    Physiologia plantarum

    2012  Volume 145, Issue 1, Page(s) 224–234

    Abstract: Degradation of periplasmic proteins (Deg)/high temperature requirement A (HtrA) proteases are ATP-independent serine endopeptidases found in almost every organism. Database searches revealed that 16 Deg paralogues are encoded by the genome of Arabidopsis ...

    Abstract Degradation of periplasmic proteins (Deg)/high temperature requirement A (HtrA) proteases are ATP-independent serine endopeptidases found in almost every organism. Database searches revealed that 16 Deg paralogues are encoded by the genome of Arabidopsis thaliana, six of which were experimentally shown to be located in chloroplasts, one in peroxisomes, one in mitochondria and one in the nucleus. Two more Deg proteases are predicted to reside in chloroplasts, five in mitochondria (one of them with a dual chloroplastidial/mitochondrial localization) and the subcellular location of one protein is uncertain. This review summarizes the current knowledge on the role of Deg proteases in maintaining protein homeostasis and protein processing in various subcompartments of the plant cell. The chloroplast Deg proteases are the best examined so far, especially with respect to their role in the degradation of photodamaged photosynthetic proteins and in biogenesis of photosystem II (PSII). A combined action of thylakoid lumen and stroma Deg proteases in the primary cleavage of photodamaged D1 protein from PSII reaction centre is discussed on the basis of a recently resolved crystal structure of plant Deg1. The peroxisomal Deg protease is a processing enzyme responsible for the cleavage of N-terminal peroxisomal targeting signals (PTSs). A. thaliana mutants lacking this enzyme show reduced peroxisomal β-oxidation, indicating for the first time the impact of protein processing on peroxisomal functions in plants. Much less data is available for mitochondrial and nuclear Deg proteases. Based on the available expression data we hypothesize a role in general protein quality control and during acquired heat resistance.
    MeSH term(s) Arabidopsis/enzymology ; Arabidopsis Proteins/metabolism ; Cell Nucleus/enzymology ; Chloroplast Proteins/metabolism ; Chloroplasts/enzymology ; Mitochondria/enzymology ; Oxidation-Reduction ; Peroxisomes/enzymology ; Peroxisomes/physiology ; Photosynthesis ; Phylogeny ; Plant Cells/enzymology ; Plant Cells/physiology ; Proteolysis ; Serine Endopeptidases/metabolism
    Chemical Substances Arabidopsis Proteins ; Chloroplast Proteins ; Deg1 protein, Arabidopsis (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-)
    Language English
    Publishing date 2012-05
    Publishing country Denmark
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2020837-6
    ISSN 1399-3054 ; 0031-9317
    ISSN (online) 1399-3054
    ISSN 0031-9317
    DOI 10.1111/j.1399-3054.2011.01533.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Deg proteases and their role in protein quality control and processing in different subcellular compartments of the plant cell

    Schuhmann, Holger / Adamska, Iwona

    Physiologia plantarum. 2012 May, v. 145, no. 1

    2012  

    Abstract: Degradation of periplasmic proteins (Deg)/high temperature requirement A (HtrA) proteases are ATP‐independent serine endopeptidases found in almost every organism. Database searches revealed that 16 Deg paralogues are encoded by the genome of Arabidopsis ...

    Abstract Degradation of periplasmic proteins (Deg)/high temperature requirement A (HtrA) proteases are ATP‐independent serine endopeptidases found in almost every organism. Database searches revealed that 16 Deg paralogues are encoded by the genome of Arabidopsis thaliana, six of which were experimentally shown to be located in chloroplasts, one in peroxisomes, one in mitochondria and one in the nucleus. Two more Deg proteases are predicted to reside in chloroplasts, five in mitochondria (one of them with a dual chloroplastidial/mitochondrial localization) and the subcellular location of one protein is uncertain. This review summarizes the current knowledge on the role of Deg proteases in maintaining protein homeostasis and protein processing in various subcompartments of the plant cell. The chloroplast Deg proteases are the best examined so far, especially with respect to their role in the degradation of photodamaged photosynthetic proteins and in biogenesis of photosystem II (PSII). A combined action of thylakoid lumen and stroma Deg proteases in the primary cleavage of photodamaged D1 protein from PSII reaction centre is discussed on the basis of a recently resolved crystal structure of plant Deg1. The peroxisomal Deg protease is a processing enzyme responsible for the cleavage of N‐terminal peroxisomal targeting signals (PTSs). A. thaliana mutants lacking this enzyme show reduced peroxisomal β‐oxidation, indicating for the first time the impact of protein processing on peroxisomal functions in plants. Much less data is available for mitochondrial and nuclear Deg proteases. Based on the available expression data we hypothesize a role in general protein quality control and during acquired heat resistance.
    Keywords Arabidopsis thaliana ; D1 protein ; crystal structure ; databases ; genome ; heat ; homeostasis ; mitochondria ; mutants ; photosystem II ; process control ; protein degradation ; proteins ; quality control ; serine proteinases ; temperature
    Language English
    Dates of publication 2012-05
    Size p. 224-234.
    Publishing place Blackwell Publishing Ltd
    Document type Article
    ZDB-ID 2020837-6
    ISSN 1399-3054 ; 0031-9317
    ISSN (online) 1399-3054
    ISSN 0031-9317
    DOI 10.1111/j.1399-3054.2011.01533.x
    Database NAL-Catalogue (AGRICOLA)

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  5. Book ; Online ; Thesis: Deg proteases in Arabidopsis thaliana

    Schuhmann, Holger [Verfasser]

    2008  

    Author's details vorgelegt von Holger Schuhmann
    Keywords Biowissenschaften, Biologie ; Life Science, Biology
    Subject code sg570
    Language English
    Document type Book ; Online ; Thesis
    Database Digital theses on the web

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  6. Article ; Online: The family of Deg/HtrA proteases in plants

    Schuhmann Holger / Huesgen Pitter F / Adamska Iwona

    BMC Plant Biology, Vol 12, Iss 1, p

    2012  Volume 52

    Abstract: Abstract Background The Deg/HtrA family of ATP-independent serine endopeptidases is present in nearly all organisms from bacteria to human and vascular plants. In recent years, multiple deg/htrA protease genes were identified in various plant genomes. ... ...

    Abstract Abstract Background The Deg/HtrA family of ATP-independent serine endopeptidases is present in nearly all organisms from bacteria to human and vascular plants. In recent years, multiple deg/htrA protease genes were identified in various plant genomes. During genome annotations most proteases were named according to the order of discovery, hence the same names were sometimes given to different types of Deg/HtrA enzymes in different plant species. This can easily lead to false inference of individual protease functions based solely on a shared name. Therefore, the existing names and classification of these proteolytic enzymes does not meet our current needs and a phylogeny-based standardized nomenclature is required. Results Using phylogenetic and domain arrangement analysis, we improved the nomenclature of the Deg/HtrA protease family, standardized protease names based on their well-established nomenclature in Arabidopsis thaliana , and clarified the evolutionary relationship between orthologous enzymes from various photosynthetic organisms across several divergent systematic groups, including dicots, a monocot, a moss and a green alga. Furthermore, we identified a “core set” of eight proteases shared by all organisms examined here that might provide all the proteolytic potential of Deg/HtrA proteases necessary for a hypothetical plant cell. Conclusions In our proposed nomenclature, the evolutionarily closest orthologs have the same protease name, simplifying scientific communication when comparing different plant species and allowing for more reliable inference of protease functions. Further, we proposed that the high number of Deg/HtrA proteases in plants is mainly due to gene duplications unique to the respective organism.
    Keywords Botany ; QK1-989 ; Science ; Q ; DOAJ:Botany ; DOAJ:Biology ; DOAJ:Biology and Life Sciences
    Subject code 580
    Language English
    Publishing date 2012-04-01T00:00:00Z
    Publisher BioMed Central
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Publisher Correction: Refinement of an ovine-based immunoglobulin therapy against SARS-CoV-2, with comparison of whole IgG versus F(ab')

    Findlay-Wilson, Stephen / Easterbrook, Linda / Smith, Sandra / Pope, Neville / Aldridge, Matthew / Humphries, Gareth / Schuhmann, Holger / Ngabo, Didier / Rayner, Emma / Otter, Ashley / Coleman, Thomas / Hicks, Bethany / Halkerston, Rachel / Apostolakis, Kostis / Taylor, Stephen / Fotheringham, Susan / Horton, Amanda / CanoCejas, Irene / Wand, Matthew /
    Tree, Julia A / Sutton, Mark / Graham, Victoria / Hewson, Roger / Dowall, Stuart

    Scientific reports

    2023  Volume 13, Issue 1, Page(s) 15419

    Language English
    Publishing date 2023-09-18
    Publishing country England
    Document type Published Erratum
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-023-42526-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Refinement of an ovine-based immunoglobulin therapy against SARS-CoV-2, with comparison of whole IgG versus F(ab')

    Findlay-Wilson, Stephen / Easterbrook, Linda / Smith, Sandra / Pope, Neville / Aldridge, Matthew / Humphries, Gareth / Schuhmann, Holger / Ngabo, Didier / Rayner, Emma / Otter, Ashley / Coleman, Thomas / Hicks, Bethany / Halkerston, Rachel / Apostolakis, Kostis / Taylor, Stephen / Fotheringham, Susan / Horton, Amanda / CanoCejas, Irene / Wand, Matthew /
    Tree, Julia A / Sutton, Mark / Graham, Victoria / Hewson, Roger / Dowall, Stuart

    Scientific reports

    2023  Volume 13, Issue 1, Page(s) 13912

    Abstract: The development of new therapies against SARS-CoV-2 is required to extend the toolkit of intervention strategies to combat the global pandemic. In this study, hyperimmune plasma from sheep immunised with whole spike SARS-CoV-2 recombinant protein has ... ...

    Abstract The development of new therapies against SARS-CoV-2 is required to extend the toolkit of intervention strategies to combat the global pandemic. In this study, hyperimmune plasma from sheep immunised with whole spike SARS-CoV-2 recombinant protein has been used to generate candidate products. In addition to purified IgG, we have refined candidate therapies by removing non-specific IgG via affinity binding along with fragmentation to eliminate the Fc region to create F(ab')
    MeSH term(s) Cricetinae ; Animals ; Sheep ; SARS-CoV-2 ; COVID-19 ; Immunization, Passive ; Kinetics ; Immunoglobulin G
    Chemical Substances Immunoglobulin G
    Language English
    Publishing date 2023-08-25
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-023-40277-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: The family of Deg/HtrA proteases in plants.

    Schuhmann, Holger / Huesgen, Pitter F / Adamska, Iwona

    BMC plant biology

    2012  Volume 12, Page(s) 52

    Abstract: Background: The Deg/HtrA family of ATP-independent serine endopeptidases is present in nearly all organisms from bacteria to human and vascular plants. In recent years, multiple deg/htrA protease genes were identified in various plant genomes. During ... ...

    Abstract Background: The Deg/HtrA family of ATP-independent serine endopeptidases is present in nearly all organisms from bacteria to human and vascular plants. In recent years, multiple deg/htrA protease genes were identified in various plant genomes. During genome annotations most proteases were named according to the order of discovery, hence the same names were sometimes given to different types of Deg/HtrA enzymes in different plant species. This can easily lead to false inference of individual protease functions based solely on a shared name. Therefore, the existing names and classification of these proteolytic enzymes does not meet our current needs and a phylogeny-based standardized nomenclature is required.
    Results: Using phylogenetic and domain arrangement analysis, we improved the nomenclature of the Deg/HtrA protease family, standardized protease names based on their well-established nomenclature in Arabidopsis thaliana, and clarified the evolutionary relationship between orthologous enzymes from various photosynthetic organisms across several divergent systematic groups, including dicots, a monocot, a moss and a green alga. Furthermore, we identified a "core set" of eight proteases shared by all organisms examined here that might provide all the proteolytic potential of Deg/HtrA proteases necessary for a hypothetical plant cell.
    Conclusions: In our proposed nomenclature, the evolutionarily closest orthologs have the same protease name, simplifying scientific communication when comparing different plant species and allowing for more reliable inference of protease functions. Further, we proposed that the high number of Deg/HtrA proteases in plants is mainly due to gene duplications unique to the respective organism.
    MeSH term(s) Amino Acid Sequence ; Catalytic Domain ; Databases, Protein ; Gene Duplication ; Genes, Plant ; Heat-Shock Proteins/chemistry ; Heat-Shock Proteins/classification ; Heat-Shock Proteins/genetics ; Molecular Sequence Data ; PDZ Domains ; Periplasmic Proteins/chemistry ; Periplasmic Proteins/classification ; Periplasmic Proteins/genetics ; Phylogeny ; Plant Proteins/chemistry ; Plant Proteins/classification ; Plant Proteins/genetics ; Plants/enzymology ; Plants/genetics ; Sequence Alignment ; Serine Endopeptidases/chemistry ; Serine Endopeptidases/classification ; Serine Endopeptidases/genetics
    Chemical Substances Heat-Shock Proteins ; Periplasmic Proteins ; Plant Proteins ; DegP protease (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-)
    Language English
    Publishing date 2012-04-20
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1471-2229
    ISSN (online) 1471-2229
    DOI 10.1186/1471-2229-12-52
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: Isolation of High-Lipid Tetraselmis suecica Strains Following Repeated UV-C Mutagenesis, FACS, and High-Throughput Growth Selection

    Lim, David K. Y / Schuhmann, Holger / Sharma, Kalpesh / Schenk, Peer M

    BioEnergy research. 2015 June, v. 8, no. 2

    2015  

    Abstract: Mutagenesis and selection of microalgae can be used for accelerated breeding of elite strains, providing a significant advantage over genetic engineering as prior biochemical and genetic information is not required. Ultraviolet (UV)-C-induced mutagenesis ...

    Abstract Mutagenesis and selection of microalgae can be used for accelerated breeding of elite strains, providing a significant advantage over genetic engineering as prior biochemical and genetic information is not required. Ultraviolet (UV)-C-induced mutagenesis combined with fluorescence-activated cell sorting (FACS) and microtiter plate reader cell density screening was used to produce Tetraselmis suecica strains with increased lipid contents without compromising on cell growth. After five rounds of mutation-selection, two dosages of UV-C (50 and >98 % lethality) yielded two improved strains (M5 and M24) that produced significantly more neutral lipids (increases of 114 and 123 %, respectively). This study highlights that repeated UV-C mutagenesis and high-throughput selection for cell growth can be a viable combined approach to improve lipid productivity in microalgae. These maybe used as elite strains for future breeding programs and as potential feedstock for biodiesel production.
    Keywords Tetraselmis suecica ; biodiesel ; breeding ; cell growth ; feedstocks ; flow cytometry ; genetic engineering ; microalgae ; mutagenesis ; screening ; triacylglycerols ; ultraviolet radiation
    Language English
    Dates of publication 2015-06
    Size p. 750-759.
    Publishing place Springer-Verlag
    Document type Article
    ZDB-ID 2424546-X
    ISSN 1939-1242 ; 1939-1234
    ISSN (online) 1939-1242
    ISSN 1939-1234
    DOI 10.1007/s12155-014-9553-2
    Database NAL-Catalogue (AGRICOLA)

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