Phosphorylation of chloroplast membrane polypeptides View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1977-09

AUTHORS

J. BENNETT

ABSTRACT

ILLUMINATION of chloroplast thylakoids leads to the formation of the so-called high energy state of the membrane1–3. The establishment of this state is accompanied by several structural changes within the membrane, including a conformational change in the coupling factor4, increased accessibility of photosystem II to the chemical probe p-diazonium benzene sulphonate5, and a reduction in the thickness of the partition between stacked thylakoids6. I describe here a rather different type of structural change that has not previously been reported for chloroplast membranes—protein phosphorylation. Like the above changes, protein phosphorylation is a reversible, energy-dependent membrane modification, but it differs from the other changes in that it takes the form of a specific chemical reaction involving certain identifiable chloroplast membrane polypeptides. The most conspicuous of these polypeptides is the light-harvesting chlorophyll a/b binding protein, the most abundant thylakoid polypeptide7. More... »

PAGES

344-346

References to SciGraph publications

  • 1972-01. Nomenclature for Isolated Chloroplasts in NATURE
  • 1975-06. Protein kinase ofAcetabularia in PROTOPLASMA
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/269344a0

    DOI

    http://dx.doi.org/10.1038/269344a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1002689737


    Indexing Status Check whether this publication has been indexed by Scopus and Web Of Science using the SN Indexing Status Tool
    Incoming Citations Browse incoming citations for this publication using opencitations.net

    JSON-LD is the canonical representation for SciGraph data.

    TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

    [
      {
        "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
        "about": [
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Biological Sciences", 
            "type": "DefinedTerm"
          }, 
          {
            "id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601", 
            "inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/", 
            "name": "Biochemistry and Cell Biology", 
            "type": "DefinedTerm"
          }
        ], 
        "author": [
          {
            "affiliation": {
              "alternateName": "Department of Biological Sciences, University of Warwick, Coventry, UK", 
              "id": "http://www.grid.ac/institutes/grid.7372.1", 
              "name": [
                "Department of Biological Sciences, University of Warwick, Coventry, UK"
              ], 
              "type": "Organization"
            }, 
            "familyName": "BENNETT", 
            "givenName": "J.", 
            "type": "Person"
          }
        ], 
        "citation": [
          {
            "id": "sg:pub.10.1007/bf01567947", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1016564890", 
              "https://doi.org/10.1007/bf01567947"
            ], 
            "type": "CreativeWork"
          }, 
          {
            "id": "sg:pub.10.1038/newbio235125a0", 
            "sameAs": [
              "https://app.dimensions.ai/details/publication/pub.1042108060", 
              "https://doi.org/10.1038/newbio235125a0"
            ], 
            "type": "CreativeWork"
          }
        ], 
        "datePublished": "1977-09", 
        "datePublishedReg": "1977-09-01", 
        "description": "ILLUMINATION of chloroplast thylakoids leads to the formation of the so-called high energy state of the membrane1\u20133. The establishment of this state is accompanied by several structural changes within the membrane, including a conformational change in the coupling factor4, increased accessibility of photosystem II to the chemical probe p-diazonium benzene sulphonate5, and a reduction in the thickness of the partition between stacked thylakoids6. I describe here a rather different type of structural change that has not previously been reported for chloroplast membranes\u2014protein phosphorylation. Like the above changes, protein phosphorylation is a reversible, energy-dependent membrane modification, but it differs from the other changes in that it takes the form of a specific chemical reaction involving certain identifiable chloroplast membrane polypeptides. The most conspicuous of these polypeptides is the light-harvesting chlorophyll a/b binding protein, the most abundant thylakoid polypeptide7.", 
        "genre": "article", 
        "id": "sg:pub.10.1038/269344a0", 
        "isAccessibleForFree": false, 
        "isPartOf": [
          {
            "id": "sg:journal.1018957", 
            "issn": [
              "0028-0836", 
              "1476-4687"
            ], 
            "name": "Nature", 
            "publisher": "Springer Nature", 
            "type": "Periodical"
          }, 
          {
            "issueNumber": "5626", 
            "type": "PublicationIssue"
          }, 
          {
            "type": "PublicationVolume", 
            "volumeNumber": "269"
          }
        ], 
        "keywords": [
          "chloroplast membrane polypeptides", 
          "membrane polypeptides", 
          "light-harvesting chlorophyll a/b", 
          "chlorophyll a/b", 
          "membrane protein phosphorylation", 
          "protein phosphorylation", 
          "photosystem II", 
          "chloroplast thylakoids", 
          "conformational changes", 
          "phosphorylation", 
          "polypeptide", 
          "membrane modification", 
          "structural changes", 
          "thylakoids", 
          "protein", 
          "membrane", 
          "specific chemical reactions", 
          "changes", 
          "establishment", 
          "above changes", 
          "modification", 
          "formation", 
          "accessibility", 
          "high-energy states", 
          "different types", 
          "types", 
          "form", 
          "energy states", 
          "chemical reactions", 
          "state", 
          "reduction", 
          "reaction", 
          "partition", 
          "illumination", 
          "thickness"
        ], 
        "name": "Phosphorylation of chloroplast membrane polypeptides", 
        "pagination": "344-346", 
        "productId": [
          {
            "name": "dimensions_id", 
            "type": "PropertyValue", 
            "value": [
              "pub.1002689737"
            ]
          }, 
          {
            "name": "doi", 
            "type": "PropertyValue", 
            "value": [
              "10.1038/269344a0"
            ]
          }
        ], 
        "sameAs": [
          "https://doi.org/10.1038/269344a0", 
          "https://app.dimensions.ai/details/publication/pub.1002689737"
        ], 
        "sdDataset": "articles", 
        "sdDatePublished": "2022-10-01T06:26", 
        "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
        "sdPublisher": {
          "name": "Springer Nature - SN SciGraph project", 
          "type": "Organization"
        }, 
        "sdSource": "s3://com-springernature-scigraph/baseset/20221001/entities/gbq_results/article/article_122.jsonl", 
        "type": "ScholarlyArticle", 
        "url": "https://doi.org/10.1038/269344a0"
      }
    ]
     

    Download the RDF metadata as:  json-ld nt turtle xml License info

    HOW TO GET THIS DATA PROGRAMMATICALLY:

    JSON-LD is a popular format for linked data which is fully compatible with JSON.

    curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/269344a0'

    N-Triples is a line-based linked data format ideal for batch operations.

    curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/269344a0'

    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/269344a0'

    RDF/XML is a standard XML format for linked data.

    curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/269344a0'


     

    This table displays all metadata directly associated to this object as RDF triples.

    99 TRIPLES      21 PREDICATES      62 URIs      52 LITERALS      6 BLANK NODES

    Subject Predicate Object
    1 sg:pub.10.1038/269344a0 schema:about anzsrc-for:06
    2 anzsrc-for:0601
    3 schema:author N7fb248c00ed3452abc76c5dbad4382bd
    4 schema:citation sg:pub.10.1007/bf01567947
    5 sg:pub.10.1038/newbio235125a0
    6 schema:datePublished 1977-09
    7 schema:datePublishedReg 1977-09-01
    8 schema:description ILLUMINATION of chloroplast thylakoids leads to the formation of the so-called high energy state of the membrane1–3. The establishment of this state is accompanied by several structural changes within the membrane, including a conformational change in the coupling factor4, increased accessibility of photosystem II to the chemical probe p-diazonium benzene sulphonate5, and a reduction in the thickness of the partition between stacked thylakoids6. I describe here a rather different type of structural change that has not previously been reported for chloroplast membranes—protein phosphorylation. Like the above changes, protein phosphorylation is a reversible, energy-dependent membrane modification, but it differs from the other changes in that it takes the form of a specific chemical reaction involving certain identifiable chloroplast membrane polypeptides. The most conspicuous of these polypeptides is the light-harvesting chlorophyll a/b binding protein, the most abundant thylakoid polypeptide7.
    9 schema:genre article
    10 schema:isAccessibleForFree false
    11 schema:isPartOf N2900365e31a1454782dd46de25417bb3
    12 N6f328a0909b942a4bc5b2e3f216ff7b3
    13 sg:journal.1018957
    14 schema:keywords above changes
    15 accessibility
    16 changes
    17 chemical reactions
    18 chlorophyll a/b
    19 chloroplast membrane polypeptides
    20 chloroplast thylakoids
    21 conformational changes
    22 different types
    23 energy states
    24 establishment
    25 form
    26 formation
    27 high-energy states
    28 illumination
    29 light-harvesting chlorophyll a/b
    30 membrane
    31 membrane modification
    32 membrane polypeptides
    33 membrane protein phosphorylation
    34 modification
    35 partition
    36 phosphorylation
    37 photosystem II
    38 polypeptide
    39 protein
    40 protein phosphorylation
    41 reaction
    42 reduction
    43 specific chemical reactions
    44 state
    45 structural changes
    46 thickness
    47 thylakoids
    48 types
    49 schema:name Phosphorylation of chloroplast membrane polypeptides
    50 schema:pagination 344-346
    51 schema:productId N913861fc06b74a8f9e58c9947ca24b1e
    52 Ne1e950d2bb584623a0f621a449c72c3c
    53 schema:sameAs https://app.dimensions.ai/details/publication/pub.1002689737
    54 https://doi.org/10.1038/269344a0
    55 schema:sdDatePublished 2022-10-01T06:26
    56 schema:sdLicense https://scigraph.springernature.com/explorer/license/
    57 schema:sdPublisher N1a6d51d2a6b244d9be516cdb1b9cc638
    58 schema:url https://doi.org/10.1038/269344a0
    59 sgo:license sg:explorer/license/
    60 sgo:sdDataset articles
    61 rdf:type schema:ScholarlyArticle
    62 N1a6d51d2a6b244d9be516cdb1b9cc638 schema:name Springer Nature - SN SciGraph project
    63 rdf:type schema:Organization
    64 N211505448fd74289afda9eb0566bb8ac schema:affiliation grid-institutes:grid.7372.1
    65 schema:familyName BENNETT
    66 schema:givenName J.
    67 rdf:type schema:Person
    68 N2900365e31a1454782dd46de25417bb3 schema:issueNumber 5626
    69 rdf:type schema:PublicationIssue
    70 N6f328a0909b942a4bc5b2e3f216ff7b3 schema:volumeNumber 269
    71 rdf:type schema:PublicationVolume
    72 N7fb248c00ed3452abc76c5dbad4382bd rdf:first N211505448fd74289afda9eb0566bb8ac
    73 rdf:rest rdf:nil
    74 N913861fc06b74a8f9e58c9947ca24b1e schema:name dimensions_id
    75 schema:value pub.1002689737
    76 rdf:type schema:PropertyValue
    77 Ne1e950d2bb584623a0f621a449c72c3c schema:name doi
    78 schema:value 10.1038/269344a0
    79 rdf:type schema:PropertyValue
    80 anzsrc-for:06 schema:inDefinedTermSet anzsrc-for:
    81 schema:name Biological Sciences
    82 rdf:type schema:DefinedTerm
    83 anzsrc-for:0601 schema:inDefinedTermSet anzsrc-for:
    84 schema:name Biochemistry and Cell Biology
    85 rdf:type schema:DefinedTerm
    86 sg:journal.1018957 schema:issn 0028-0836
    87 1476-4687
    88 schema:name Nature
    89 schema:publisher Springer Nature
    90 rdf:type schema:Periodical
    91 sg:pub.10.1007/bf01567947 schema:sameAs https://app.dimensions.ai/details/publication/pub.1016564890
    92 https://doi.org/10.1007/bf01567947
    93 rdf:type schema:CreativeWork
    94 sg:pub.10.1038/newbio235125a0 schema:sameAs https://app.dimensions.ai/details/publication/pub.1042108060
    95 https://doi.org/10.1038/newbio235125a0
    96 rdf:type schema:CreativeWork
    97 grid-institutes:grid.7372.1 schema:alternateName Department of Biological Sciences, University of Warwick, Coventry, UK
    98 schema:name Department of Biological Sciences, University of Warwick, Coventry, UK
    99 rdf:type schema:Organization
     




    Preview window. Press ESC to close (or click here)


    ...