Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II
Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutan...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Leto, Kenneth J. [verfasserIn] Bell, Erin [verfasserIn] McIntosh, Lee [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1985 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 1985 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 4(1985), 7 vom: 01. Juli, Seite 1645-1653 |
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| Übergeordnetes Werk: |
volume:4 ; year:1985 ; number:7 ; day:01 ; month:07 ; pages:1645-1653 |
| Links: |
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| DOI / URN: |
10.1002/j.1460-2075.1985.tb03832.x |
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SPR057556210 |
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| 100 | 1 | |a Leto, Kenneth J. |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II |
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| 520 | |a Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. | ||
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| 650 | 4 | |a thylakoid membrane |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a 34.5 kd polypeptide |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Bell, Erin |e verfasserin |4 aut | |
| 700 | 1 | |a McIntosh, Lee |e verfasserin |4 aut | |
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10.1002/j.1460-2075.1985.tb03832.x doi (DE-627)SPR057556210 (SPR)j.1460-2075.1985.tb03832.x-e DE-627 ger DE-627 rakwb eng Leto, Kenneth J. verfasserin aut Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II 1985 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1985 Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. photosystem II polypeptides (dpeaa)DE-He213 thylakoid protein synthesis (dpeaa)DE-He213 thylakoid protein turnover (dpeaa)DE-He213 thylakoid membrane (dpeaa)DE-He213 34.5 kd polypeptide (dpeaa)DE-He213 Bell, Erin verfasserin aut McIntosh, Lee verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 4(1985), 7 vom: 01. Juli, Seite 1645-1653 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:4 year:1985 number:7 day:01 month:07 pages:1645-1653 https://dx.doi.org/10.1002/j.1460-2075.1985.tb03832.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 1985 7 01 07 1645-1653 |
| spelling |
10.1002/j.1460-2075.1985.tb03832.x doi (DE-627)SPR057556210 (SPR)j.1460-2075.1985.tb03832.x-e DE-627 ger DE-627 rakwb eng Leto, Kenneth J. verfasserin aut Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II 1985 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1985 Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. photosystem II polypeptides (dpeaa)DE-He213 thylakoid protein synthesis (dpeaa)DE-He213 thylakoid protein turnover (dpeaa)DE-He213 thylakoid membrane (dpeaa)DE-He213 34.5 kd polypeptide (dpeaa)DE-He213 Bell, Erin verfasserin aut McIntosh, Lee verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 4(1985), 7 vom: 01. Juli, Seite 1645-1653 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:4 year:1985 number:7 day:01 month:07 pages:1645-1653 https://dx.doi.org/10.1002/j.1460-2075.1985.tb03832.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 1985 7 01 07 1645-1653 |
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10.1002/j.1460-2075.1985.tb03832.x doi (DE-627)SPR057556210 (SPR)j.1460-2075.1985.tb03832.x-e DE-627 ger DE-627 rakwb eng Leto, Kenneth J. verfasserin aut Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II 1985 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1985 Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. photosystem II polypeptides (dpeaa)DE-He213 thylakoid protein synthesis (dpeaa)DE-He213 thylakoid protein turnover (dpeaa)DE-He213 thylakoid membrane (dpeaa)DE-He213 34.5 kd polypeptide (dpeaa)DE-He213 Bell, Erin verfasserin aut McIntosh, Lee verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 4(1985), 7 vom: 01. Juli, Seite 1645-1653 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:4 year:1985 number:7 day:01 month:07 pages:1645-1653 https://dx.doi.org/10.1002/j.1460-2075.1985.tb03832.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 1985 7 01 07 1645-1653 |
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10.1002/j.1460-2075.1985.tb03832.x doi (DE-627)SPR057556210 (SPR)j.1460-2075.1985.tb03832.x-e DE-627 ger DE-627 rakwb eng Leto, Kenneth J. verfasserin aut Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II 1985 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1985 Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. photosystem II polypeptides (dpeaa)DE-He213 thylakoid protein synthesis (dpeaa)DE-He213 thylakoid protein turnover (dpeaa)DE-He213 thylakoid membrane (dpeaa)DE-He213 34.5 kd polypeptide (dpeaa)DE-He213 Bell, Erin verfasserin aut McIntosh, Lee verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 4(1985), 7 vom: 01. Juli, Seite 1645-1653 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:4 year:1985 number:7 day:01 month:07 pages:1645-1653 https://dx.doi.org/10.1002/j.1460-2075.1985.tb03832.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 1985 7 01 07 1645-1653 |
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10.1002/j.1460-2075.1985.tb03832.x doi (DE-627)SPR057556210 (SPR)j.1460-2075.1985.tb03832.x-e DE-627 ger DE-627 rakwb eng Leto, Kenneth J. verfasserin aut Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II 1985 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1985 Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. photosystem II polypeptides (dpeaa)DE-He213 thylakoid protein synthesis (dpeaa)DE-He213 thylakoid protein turnover (dpeaa)DE-He213 thylakoid membrane (dpeaa)DE-He213 34.5 kd polypeptide (dpeaa)DE-He213 Bell, Erin verfasserin aut McIntosh, Lee verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 4(1985), 7 vom: 01. Juli, Seite 1645-1653 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:4 year:1985 number:7 day:01 month:07 pages:1645-1653 https://dx.doi.org/10.1002/j.1460-2075.1985.tb03832.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 1985 7 01 07 1645-1653 |
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Leto, Kenneth J. |
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Leto, Kenneth J. misc photosystem II polypeptides misc thylakoid protein synthesis misc thylakoid protein turnover misc thylakoid membrane misc 34.5 kd polypeptide Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II |
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Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II photosystem II polypeptides (dpeaa)DE-He213 thylakoid protein synthesis (dpeaa)DE-He213 thylakoid protein turnover (dpeaa)DE-He213 thylakoid membrane (dpeaa)DE-He213 34.5 kd polypeptide (dpeaa)DE-He213 |
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Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II |
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nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem ii |
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Nuclear mutation leads to an accelerated turnover of chloroplast‐encoded 48 kd and 34.5 kd polypeptides in thylakoids lacking photosystem II |
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Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. © European Molecular Biology Organization 1985 |
| abstractGer |
Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. © European Molecular Biology Organization 1985 |
| abstract_unstemmed |
Abstract We have studied the synthesis and accumulation of a chloroplast‐encoded 48 kd chla‐reaction center protein and the 34.5 kd ‘atrazine binding’ protein in a nuclear maize mutant which fails to assemble photosystem II reaction centers. The failure of these polypeptides to accumulation in mutant thylakoids is not due to direct nuclear control over their synthesis but is rather due to their specific, accelerated turnover from the thylakoid membrane. The accelerated turnover of these polypeptides in mutant thylakoids is largely independent of illumination conditions, as accelerated turnover occurs in the dark as well as in the light. In contrast to wild type, the 48 kd and 34.5 kd polypeptides are preferentially associated with stroma, rather than grana, lamellae in mutant membranes, suggesting that turnover occurs before these polypeptides become enriched in the grana. The nucleus thus plays a role in the stabilization of these chloroplast‐encoded photosystem II reaction center polypeptides. © European Molecular Biology Organization 1985 |
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