The yeast split-ubiquitin system to study chloroplast membrane protein interactions
Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and the...
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| Autor*in: |
Pasch, Jan Christoph [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2005 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer-Verlag 2005 |
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| Übergeordnetes Werk: |
Enthalten in: Applied microbiology and biotechnology - Springer Berlin Heidelberg, 1984, 69(2005), 4 vom: 30. Juni, Seite 440-447 |
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| Übergeordnetes Werk: |
volume:69 ; year:2005 ; number:4 ; day:30 ; month:06 ; pages:440-447 |
| Links: |
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| DOI / URN: |
10.1007/s00253-005-0029-3 |
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| 520 | |a Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. | ||
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10.1007/s00253-005-0029-3 doi (DE-627)OLC2050704615 (DE-He213)s00253-005-0029-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Pasch, Jan Christoph verfasserin aut The yeast split-ubiquitin system to study chloroplast membrane protein interactions 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. Yeast Cell Thylakoid Membrane Synechocystis Reaction Center Protein Thylakoid Membrane Protein Nickelsen, Jörg aut Schünemann, Danja aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 4 vom: 30. Juni, Seite 440-447 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:4 day:30 month:06 pages:440-447 https://doi.org/10.1007/s00253-005-0029-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 4 30 06 440-447 |
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10.1007/s00253-005-0029-3 doi (DE-627)OLC2050704615 (DE-He213)s00253-005-0029-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Pasch, Jan Christoph verfasserin aut The yeast split-ubiquitin system to study chloroplast membrane protein interactions 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. Yeast Cell Thylakoid Membrane Synechocystis Reaction Center Protein Thylakoid Membrane Protein Nickelsen, Jörg aut Schünemann, Danja aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 4 vom: 30. Juni, Seite 440-447 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:4 day:30 month:06 pages:440-447 https://doi.org/10.1007/s00253-005-0029-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 4 30 06 440-447 |
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10.1007/s00253-005-0029-3 doi (DE-627)OLC2050704615 (DE-He213)s00253-005-0029-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Pasch, Jan Christoph verfasserin aut The yeast split-ubiquitin system to study chloroplast membrane protein interactions 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. Yeast Cell Thylakoid Membrane Synechocystis Reaction Center Protein Thylakoid Membrane Protein Nickelsen, Jörg aut Schünemann, Danja aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 4 vom: 30. Juni, Seite 440-447 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:4 day:30 month:06 pages:440-447 https://doi.org/10.1007/s00253-005-0029-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 4 30 06 440-447 |
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10.1007/s00253-005-0029-3 doi (DE-627)OLC2050704615 (DE-He213)s00253-005-0029-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Pasch, Jan Christoph verfasserin aut The yeast split-ubiquitin system to study chloroplast membrane protein interactions 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. Yeast Cell Thylakoid Membrane Synechocystis Reaction Center Protein Thylakoid Membrane Protein Nickelsen, Jörg aut Schünemann, Danja aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 4 vom: 30. Juni, Seite 440-447 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:4 day:30 month:06 pages:440-447 https://doi.org/10.1007/s00253-005-0029-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 4 30 06 440-447 |
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10.1007/s00253-005-0029-3 doi (DE-627)OLC2050704615 (DE-He213)s00253-005-0029-3-p DE-627 ger DE-627 rakwb eng 570 VZ 12 ssgn BIODIV DE-30 fid Pasch, Jan Christoph verfasserin aut The yeast split-ubiquitin system to study chloroplast membrane protein interactions 2005 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 2005 Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. Yeast Cell Thylakoid Membrane Synechocystis Reaction Center Protein Thylakoid Membrane Protein Nickelsen, Jörg aut Schünemann, Danja aut Enthalten in Applied microbiology and biotechnology Springer Berlin Heidelberg, 1984 69(2005), 4 vom: 30. Juni, Seite 440-447 (DE-627)129942634 (DE-600)392453-1 (DE-576)015507750 0175-7598 nnns volume:69 year:2005 number:4 day:30 month:06 pages:440-447 https://doi.org/10.1007/s00253-005-0029-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_100 GBV_ILN_130 GBV_ILN_147 GBV_ILN_267 GBV_ILN_285 GBV_ILN_2004 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4155 GBV_ILN_4277 GBV_ILN_4305 GBV_ILN_4307 AR 69 2005 4 30 06 440-447 |
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Enthalten in Applied microbiology and biotechnology 69(2005), 4 vom: 30. Juni, Seite 440-447 volume:69 year:2005 number:4 day:30 month:06 pages:440-447 |
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Enthalten in Applied microbiology and biotechnology 69(2005), 4 vom: 30. Juni, Seite 440-447 volume:69 year:2005 number:4 day:30 month:06 pages:440-447 |
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the yeast split-ubiquitin system to study chloroplast membrane protein interactions |
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The yeast split-ubiquitin system to study chloroplast membrane protein interactions |
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Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. © Springer-Verlag 2005 |
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Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. © Springer-Verlag 2005 |
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Abstract Each photosynthetic complex within the thylakoid membrane consists of several different subunits. During formation of these complexes, numerous regulatory factors are required for the coordinated transport and assembly of the subunits. Interactions between transport/assembly factors and their specific polypeptides occur in a membraneous environment and are usually transient and short-lived. Thus, a detailed analysis of the underlying molecular mechanisms by biochemical techniques is often difficult to perform. Here, we report on the suitability of a genetic system, i.e. the yeast split-ubiquitin system, to investigate protein–protein interactions of thylakoid membrane proteins. The data confirm the previously established binding of the cpSec-translocase subunits, cpSecY and cpSecE, and the interaction of the cpSec-translocase from Arabidopsis thaliana with Alb3, a factor required for the insertion of the light-harvesting chlorophyll-binding proteins into the thylakoid membrane. In addition, the proposed interaction between D1, the reaction center protein of photosystem II and the soluble periplasmic PratA factor from Synechocystis sp. PCC 6803 was verified. A more comprehensive analysis of Alb3-interacting proteins revealed that Alb3 is able to form dimers or oligomers. Interestingly, Alb3 was also shown to bind to the PSII proteins D1, D2 and CP43, to the PSI reaction center protein PSI-A and the ATP synthase subunit $ CF_{0} $III, suggesting an important role of Alb3 in the assembly of photosynthetic thylakoid membrane complexes. © Springer-Verlag 2005 |
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