Chemistry, clones, and circadian control of the dinoflagellate bioluminescent system. The Marlene DeLuca memorial lecture
Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain...
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| Autor*in: |
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1989 |
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| Umfang: |
6 Ill. 8 |
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| Reproduktion: |
Wiley InterScience Backfile Collection 1832-2000 |
|---|---|
| Übergeordnetes Werk: |
in: Journal of Bioluminescence and Chemiluminescence - New York : Wiley International, 4(1989) vom: Jan., Seite 12-19 |
| Übergeordnetes Werk: |
volume:4 ; year:1989 ; month:01 ; pages:12-19 ; extent:8 |
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| 520 | |a Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation. | ||
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(DE-627)NLEJ159374162 DE-627 ger DE-627 rakwb eng Chemistry, clones, and circadian control of the dinoflagellate bioluminescent system. The Marlene DeLuca memorial lecture 1989 6 Ill. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation. Wiley InterScience Backfile Collection 1832-2000 Hastings, J. Woodland oth in Journal of Bioluminescence and Chemiluminescence New York : Wiley International 4(1989) vom: Jan., Seite 12-19 (DE-627)NLEJ159070538 (DE-600)2001815-0 0884-3996 nnns volume:4 year:1989 month:01 pages:12-19 extent:8 http://dx.doi.org/10.1002/bio.1170040105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1989 1 12-19 8 |
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(DE-627)NLEJ159374162 DE-627 ger DE-627 rakwb eng Chemistry, clones, and circadian control of the dinoflagellate bioluminescent system. The Marlene DeLuca memorial lecture 1989 6 Ill. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation. Wiley InterScience Backfile Collection 1832-2000 Hastings, J. Woodland oth in Journal of Bioluminescence and Chemiluminescence New York : Wiley International 4(1989) vom: Jan., Seite 12-19 (DE-627)NLEJ159070538 (DE-600)2001815-0 0884-3996 nnns volume:4 year:1989 month:01 pages:12-19 extent:8 http://dx.doi.org/10.1002/bio.1170040105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1989 1 12-19 8 |
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(DE-627)NLEJ159374162 DE-627 ger DE-627 rakwb eng Chemistry, clones, and circadian control of the dinoflagellate bioluminescent system. The Marlene DeLuca memorial lecture 1989 6 Ill. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation. Wiley InterScience Backfile Collection 1832-2000 Hastings, J. Woodland oth in Journal of Bioluminescence and Chemiluminescence New York : Wiley International 4(1989) vom: Jan., Seite 12-19 (DE-627)NLEJ159070538 (DE-600)2001815-0 0884-3996 nnns volume:4 year:1989 month:01 pages:12-19 extent:8 http://dx.doi.org/10.1002/bio.1170040105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1989 1 12-19 8 |
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(DE-627)NLEJ159374162 DE-627 ger DE-627 rakwb eng Chemistry, clones, and circadian control of the dinoflagellate bioluminescent system. The Marlene DeLuca memorial lecture 1989 6 Ill. 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation. Wiley InterScience Backfile Collection 1832-2000 Hastings, J. Woodland oth in Journal of Bioluminescence and Chemiluminescence New York : Wiley International 4(1989) vom: Jan., Seite 12-19 (DE-627)NLEJ159070538 (DE-600)2001815-0 0884-3996 nnns volume:4 year:1989 month:01 pages:12-19 extent:8 http://dx.doi.org/10.1002/bio.1170040105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 4 1989 1 12-19 8 |
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Chemistry, clones, and circadian control of the dinoflagellate bioluminescent system. The Marlene DeLuca memorial lecture |
| abstract |
Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation. |
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Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation. |
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Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ159374162</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230506091307.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070201s1989 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ159374162</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Chemistry, clones, and circadian control of the dinoflagellate bioluminescent system. The Marlene DeLuca memorial lecture</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1989</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="b">6 Ill.</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">8</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Bioluminescence in the dinoflagellate Gonyaulax polyedra occurs as brief bright flashes, originating from many (∼400) small (∼0.5 μm) cytoplasmic organelles which protrude into the acidic vacuole, and are thus surrounded by the tonoplast. Biochemically, the substrate is unusual; it is an open chain tetrapyrrole, highly unstable to air but protected in the cell at pH̃ 8 by virtue of a luciferin binding protein (LBP). This molecule is a dimer of 72 kDa subunits which, upon a decrease in pH, releases luciferin to react with oxygen in the luciferase (∼140 kDa) catalysed luminescent reaction. cDNAs for both luciferase and LBP have been isolated and cloned, and the identity of LBP was confirmed by hybrid selection and in vitro translation of the message. The tenfold circadian (day to night) change in the amount of LBP, which parallels the in vivo rhythm of luminescence, is due to de novo synthesis and subsequent degradation of the protein each day. The LBP mRNA levels, as determined by in vitro translations and by Northern hybridizations, do not vary over the daily cycle, indicating that circadian control of bioluminescence in this species is mediated at the level of translation.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Wiley InterScience Backfile Collection 1832-2000</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hastings, J. Woodland</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of Bioluminescence and Chemiluminescence</subfield><subfield code="d">New York : Wiley International</subfield><subfield code="g">4(1989) vom: Jan., Seite 12-19</subfield><subfield code="w">(DE-627)NLEJ159070538</subfield><subfield code="w">(DE-600)2001815-0</subfield><subfield code="x">0884-3996</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:4</subfield><subfield code="g">year:1989</subfield><subfield code="g">month:01</subfield><subfield code="g">pages:12-19</subfield><subfield code="g">extent:8</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1002/bio.1170040105</subfield><subfield code="q">text/html</subfield><subfield code="z">Deutschlandweit zugänglich</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-WIS</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">4</subfield><subfield code="j">1989</subfield><subfield code="c">1</subfield><subfield code="h">12-19</subfield><subfield code="g">8</subfield></datafield></record></collection>
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7.399482 |