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  1. Article ; Online: The buck stops with spermidine.

    Michael, Anthony J

    Nature chemical biology

    2024  

    Language English
    Publishing date 2024-01-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/s41589-023-01510-3
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  2. Article ; Online: Sensing spermidine through tongue-tied translation prevents too much of a good thing.

    Michael, Anthony J

    Molecular cell

    2021  Volume 81, Issue 19, Page(s) 3882–3883

    Abstract: Vindu et al. (2021) identify the yeast high-affinity spermidine transporter, elucidate the mRNA uORF/eIF5a-based translational mechanism by which spermidine levels are sensed, and demonstrate that excess spermidine competitively inhibits eIF5a function, ... ...

    Abstract Vindu et al. (2021) identify the yeast high-affinity spermidine transporter, elucidate the mRNA uORF/eIF5a-based translational mechanism by which spermidine levels are sensed, and demonstrate that excess spermidine competitively inhibits eIF5a function, resulting in decreased spermidine uptake.
    MeSH term(s) Peptide Initiation Factors ; Saccharomyces cerevisiae ; Spermidine ; Tongue
    Chemical Substances Peptide Initiation Factors ; Spermidine (U87FK77H25)
    Language English
    Publishing date 2021-11-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.09.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Book: Climate change and the health of nations

    McMichael, Anthony J. / Woodward, Alistair / Muir, Cameron

    famines, fevers, and the fate of populations

    2017  

    Author's details Anthony J. McMichael with Alistair Woodward and Cameron Muir
    Keywords Human beings/Effect of climate on ; Climate and civilization/History ; Climatic changes
    Subject code 304.25
    Language English
    Size xx, 370 Seiten, Illustrationen, Diagramme, Karten, 24 cm
    Publisher Oxford University Press
    Publishing place Oxford
    Publishing country United States
    Document type Book
    HBZ-ID HT019077266
    ISBN 978-0-19-026295-2 ; 0-19-026295-8
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2017 A 512 available for loan (reading room) Lesesaal EG

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  4. Article: Sensing spermidine through tongue-tied translation prevents too much of a good thing

    Michael, Anthony J.

    Molecular cell. 2021 Oct. 07, v. 81, no. 19

    2021  

    Abstract: Vindu et al. (2021) identify the yeast high-affinity spermidine transporter, elucidate the mRNA uORF/eIF5a-based translational mechanism by which spermidine levels are sensed, and demonstrate that excess spermidine competitively inhibits eIF5a function, ... ...

    Abstract Vindu et al. (2021) identify the yeast high-affinity spermidine transporter, elucidate the mRNA uORF/eIF5a-based translational mechanism by which spermidine levels are sensed, and demonstrate that excess spermidine competitively inhibits eIF5a function, resulting in decreased spermidine uptake.
    Keywords cells ; spermidine ; transporters ; yeasts
    Language English
    Dates of publication 2021-1007
    Size p. 3882-3883.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.09.014
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: Polyamine function in archaea and bacteria.

    Michael, Anthony J

    The Journal of biological chemistry

    2018  Volume 293, Issue 48, Page(s) 18693–18701

    Abstract: Most of the phylogenetic diversity of life is found in bacteria and archaea, and is reflected in the diverse metabolism and functions of bacterial and archaeal polyamines. The polyamine spermidine was probably present in the last universal common ... ...

    Abstract Most of the phylogenetic diversity of life is found in bacteria and archaea, and is reflected in the diverse metabolism and functions of bacterial and archaeal polyamines. The polyamine spermidine was probably present in the last universal common ancestor, and polyamines are known to be necessary for critical physiological functions in bacteria, such as growth, biofilm formation, and other surface behaviors, and production of natural products, such as siderophores. There is also phylogenetic diversity of function, indicated by the role of polyamines in planktonic growth of different species, ranging from absolutely essential to entirely dispensable. However, the cellular molecular mechanisms responsible for polyamine function in bacterial growth are almost entirely unknown. In contrast, the molecular mechanisms of essential polyamine functions in archaea are better understood: covalent modification by polyamines of translation factor aIF5A and the agmatine modification of tRNA
    MeSH term(s) Archaea/chemistry ; Archaea/genetics ; Archaea/growth & development ; Archaea/metabolism ; Archaeal Proteins/genetics ; Archaeal Proteins/metabolism ; Bacteria/chemistry ; Bacteria/genetics ; Bacteria/growth & development ; Bacteria/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Polyamines/chemistry ; Polyamines/metabolism
    Chemical Substances Archaeal Proteins ; Bacterial Proteins ; Polyamines
    Language English
    Publishing date 2018-09-25
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.TM118.005670
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Functional identification of bacterial spermine, thermospermine, norspermine, norspermidine, spermidine, and N

    Li, Bin / Liang, Jue / Baniasadi, Hamid R / Kurihara, Shin / Phillips, Margaret A / Michael, Anthony J

    The Journal of biological chemistry

    2024  , Page(s) 107281

    Abstract: Spermine synthase is an aminopropyltransferase that adds an aminopropyl group to the essential polyamine spermidine to form tetraamine spermine, needed for normal human neural development, plant salt and drought resistance, and yeast CoA biosynthesis. We ...

    Abstract Spermine synthase is an aminopropyltransferase that adds an aminopropyl group to the essential polyamine spermidine to form tetraamine spermine, needed for normal human neural development, plant salt and drought resistance, and yeast CoA biosynthesis. We functionally identify for the first time bacterial spermine synthases, derived from phyla Bacillota, Rhodothermota, Thermodesulfobacteriota, Nitrospirota, Deinococcota and Pseudomonadota. We also identify bacterial aminopropyltransferases that synthesize the spermine same mass isomer thermospermine, from phyla Cyanobacteriota, Thermodesulfobacteriota, Nitrospirota, Dictyoglomota, Armatimonadota and Pseudomonadota, including the human opportunistic pathogen Pseudomonas aeruginosa. Most of these bacterial synthases were capable of synthesizing spermine or thermospermine from the diamine putrescine, and so possess also spermidine synthase activity. We found that most thermospermine synthases could synthesize tetraamine norspermine from triamine norspermidine, i.e., they are potential norspermine synthases. This finding could explain the enigmatic source of norspermine in bacteria. Some of the thermospermine synthases could synthesize norspermidine from diamine 1,3-diaminopropane, demonstrating that they are potential norspermidine synthases. Of 18 bacterial spermidine synthases identified, 17 were able to aminopropylate agmatine to form N
    Language English
    Publishing date 2024-04-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2024.107281
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  7. Article ; Online: Evolution of biosynthetic diversity.

    Michael, Anthony J

    The Biochemical journal

    2017  Volume 474, Issue 14, Page(s) 2277–2299

    Abstract: Since the emergence of the last common ancestor from which all extant life evolved, the metabolite repertoire of cells has increased and diversified. Not only has the metabolite cosmos expanded, but the ways in which the same metabolites are made have ... ...

    Abstract Since the emergence of the last common ancestor from which all extant life evolved, the metabolite repertoire of cells has increased and diversified. Not only has the metabolite cosmos expanded, but the ways in which the same metabolites are made have diversified. Enzymes catalyzing the same reaction have evolved independently from different protein folds; the same protein fold can produce enzymes recognizing different substrates, and enzymes performing different chemistries. Genes encoding useful enzymes can be transferred between organisms and even between the major domains of life. Organisms that live in metabolite-rich environments sometimes lose the pathways that produce those same metabolites. Fusion of different protein domains results in enzymes with novel properties. This review will consider the major evolutionary mechanisms that generate biosynthetic diversity: gene duplication (and gene loss), horizontal and endosymbiotic gene transfer, and gene fusion. It will also discuss mechanisms that lead to convergence as well as divergence. To illustrate these mechanisms, one of the original metabolisms present in the last universal common ancestor will be employed: polyamine metabolism, which is essential for the growth and cell proliferation of archaea and eukaryotes, and many bacteria.
    MeSH term(s) Animals ; Biocatalysis ; Biodiversity ; Ecological and Environmental Phenomena ; Enzymes/chemistry ; Enzymes/genetics ; Enzymes/metabolism ; Evolution, Molecular ; Gene Deletion ; Gene Duplication ; Gene Fusion ; Gene Transfer, Horizontal ; Humans ; Models, Molecular ; Polyamines/metabolism ; Protein Biosynthesis ; Protein Folding ; Structural Homology, Protein ; Symbiosis
    Chemical Substances Enzymes ; Polyamines
    Language English
    Publishing date 2017-06-27
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20160823
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Neofunctionalization of S-adenosylmethionine decarboxylase into pyruvoyl-dependent L-ornithine and L-arginine decarboxylases is widespread in bacteria and archaea.

    Li, Bin / Liang, Jue / Phillips, Margaret A / Michael, Anthony J

    The Journal of biological chemistry

    2023  Volume 299, Issue 8, Page(s) 105005

    Abstract: S-adenosylmethionine decarboxylase (AdoMetDC/SpeD) is a key polyamine biosynthetic enzyme required for conversion of putrescine to spermidine. Autocatalytic self-processing of the AdoMetDC/SpeD proenzyme generates a pyruvoyl cofactor from an internal ... ...

    Abstract S-adenosylmethionine decarboxylase (AdoMetDC/SpeD) is a key polyamine biosynthetic enzyme required for conversion of putrescine to spermidine. Autocatalytic self-processing of the AdoMetDC/SpeD proenzyme generates a pyruvoyl cofactor from an internal serine. Recently, we discovered that diverse bacteriophages encode AdoMetDC/SpeD homologs that lack AdoMetDC activity and instead decarboxylate L-ornithine or L-arginine. We reasoned that neofunctionalized AdoMetDC/SpeD homologs were unlikely to have emerged in bacteriophages and were probably acquired from ancestral bacterial hosts. To test this hypothesis, we sought to identify candidate AdoMetDC/SpeD homologs encoding L-ornithine and L-arginine decarboxylases in bacteria and archaea. We searched for the anomalous presence of AdoMetDC/SpeD homologs in the absence of its obligatory partner enzyme spermidine synthase, or the presence of two AdoMetDC/SpeD homologs encoded in the same genome. Biochemical characterization of candidate neofunctionalized genes confirmed lack of AdoMetDC activity, and functional presence of L-ornithine or L-arginine decarboxylase activity in proteins from phyla Actinomycetota, Armatimonadota, Planctomycetota, Melainabacteria, Perigrinibacteria, Atribacteria, Chloroflexota, Sumerlaeota, Omnitrophota, Lentisphaerota, and Euryarchaeota, the bacterial candidate phyla radiation and DPANN archaea, and the δ-Proteobacteria class. Phylogenetic analysis indicated that L-arginine decarboxylases emerged at least three times from AdoMetDC/SpeD, whereas L-ornithine decarboxylases arose only once, potentially from the AdoMetDC/SpeD-derived L-arginine decarboxylases, revealing unsuspected polyamine metabolic plasticity. Horizontal transfer of the neofunctionalized genes appears to be the more prevalent mode of dissemination. We identified fusion proteins of bona fide AdoMetDC/SpeD with homologous L-ornithine decarboxylases that possess two, unprecedented internal protein-derived pyruvoyl cofactors. These fusion proteins suggest a plausible model for the evolution of the eukaryotic AdoMetDC.
    MeSH term(s) Adenosylmethionine Decarboxylase/genetics ; Adenosylmethionine Decarboxylase/metabolism ; Archaea/genetics ; Archaea/metabolism ; Ornithine ; Phylogeny ; Carboxy-Lyases/genetics ; Carboxy-Lyases/metabolism ; Polyamines/metabolism ; Bacteria/metabolism ; Ornithine Decarboxylase/metabolism ; Arginine/genetics
    Chemical Substances arginine decarboxylase (EC 4.1.1.19) ; Adenosylmethionine Decarboxylase (EC 4.1.1.50) ; Ornithine (E524N2IXA3) ; Carboxy-Lyases (EC 4.1.1.-) ; Polyamines ; Ornithine Decarboxylase (EC 4.1.1.17) ; Arginine (94ZLA3W45F)
    Language English
    Publishing date 2023-07-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2023.105005
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Biosynthesis of polyamines and polyamine-containing molecules.

    Michael, Anthony J

    The Biochemical journal

    2016  Volume 473, Issue 15, Page(s) 2315–2329

    Abstract: Polyamines are evolutionarily ancient polycations derived from amino acids and are pervasive in all domains of life. They are essential for cell growth and proliferation in eukaryotes and are essential, important or dispensable for growth in bacteria. ... ...

    Abstract Polyamines are evolutionarily ancient polycations derived from amino acids and are pervasive in all domains of life. They are essential for cell growth and proliferation in eukaryotes and are essential, important or dispensable for growth in bacteria. Polyamines present a useful scaffold to attach other moieties to, and are often incorporated into specialized metabolism. Life has evolved multiple pathways to synthesize polyamines, and structural variants of polyamines have evolved in bacteria, archaea and eukaryotes. Among the complex biosynthetic diversity, patterns of evolutionary reiteration can be distinguished, revealing evolutionary recycling of particular protein folds and enzyme chassis. The same enzyme activities have evolved from multiple protein folds, suggesting an inevitability of evolution of polyamine biosynthesis. This review discusses the different biosynthetic strategies used in life to produce diamines, triamines, tetra-amines and branched and long-chain polyamines. It also discusses the enzymes that incorporate polyamines into specialized metabolites and attempts to place polyamine biosynthesis in an evolutionary context.
    MeSH term(s) Animals ; Archaea/metabolism ; Bacteria/metabolism ; Biological Evolution ; Humans ; Polyamines/metabolism
    Chemical Substances Polyamines
    Language English
    Publishing date 2016-08-01
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20160185
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  10. Article ; Online: Polyamines in Eukaryotes, Bacteria, and Archaea.

    Michael, Anthony J

    The Journal of biological chemistry

    2016  Volume 291, Issue 29, Page(s) 14896–14903

    Abstract: Polyamines are primordial polycations found in most cells and perform different functions in different organisms. Although polyamines are mainly known for their essential roles in cell growth and proliferation, their functions range from a critical role ... ...

    Abstract Polyamines are primordial polycations found in most cells and perform different functions in different organisms. Although polyamines are mainly known for their essential roles in cell growth and proliferation, their functions range from a critical role in cellular translation in eukaryotes and archaea, to bacterial biofilm formation and specialized roles in natural product biosynthesis. At first glance, the diversity of polyamine structures in different organisms appears chaotic; however, biosynthetic flexibility and evolutionary and ecological processes largely explain this heterogeneity. In this review, I discuss the biosynthetic, evolutionary, and physiological processes that constrain or expand polyamine structural and functional diversity.
    MeSH term(s) Archaea/metabolism ; Bacteria/metabolism ; Biosynthetic Pathways ; Eukaryota/metabolism ; Gene Transfer, Horizontal/genetics ; Polyamines/metabolism
    Chemical Substances Polyamines
    Language English
    Publishing date 2016-06-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.R116.734780
    Database MEDical Literature Analysis and Retrieval System OnLINE

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