Kooperativer Bibliotheksverbund

Berlin Brandenburg

X
and
and

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Type of Medium
Language
Year
Person/Organisation
Topic
Source
Journal
  • 1
    Article
    Article
    Thylakoid membrane reduction affects the photosystem stoichiometry in the cyanobacterium Synechocystis sp. PCC 6803 (2009)
    Details
    Language: English
    In: Plant physiology, February 2009, Vol.149(2), pp.735-44
    Description: Biogenesis of thylakoid membranes in both chloroplasts and cyanobacteria is largely not understood today. The vesicle-inducing protein in plastids 1 (Vipp1) has been suggested to be essential for thylakoid membrane formation in Arabidopsis (Arabidopsis thaliana), as well as in the cyanobacterium Synechocystis sp. PCC 6803, although its exact physiological function remains elusive so far. Here, we report that, upon depletion of Vipp1 in Synechocystis cells, the number of thylakoid layers in individual Synechocystis cells decreased, and that, in particular, the content of photosystem I (PSI) complexes was highly diminished in thylakoids. Furthermore, separation of native photosynthetic complexes indicated that PSI trimers are destabilized and the monomeric species is enriched. Therefore, depletion of thylakoid membranes specifically affects biogenesis and/or stabilization of PSI in cyanobacteria.
    Keywords: Synechocystis -- Metabolism ; Thylakoids -- Metabolism
    ISSN: 0032-0889
    E-ISSN: 15322548
    DOI: 10.1104/pp.108.132373
    URL: View this record in MEDLINE/PubMed
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
    Open Access Request
  • 2
    Article
    Article
    Putative function of cytochrome b559 as a plastoquinol oxidase.(Report) (2010)
    Details
    Language: English
    In: Physiologia Plantarum, April, 2010, Vol.138, p.463(11)
    Description: To authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1111/j.1399-3054.2009.01312.x Byline: Natallia Bondarava (a), Christine M. Gross (b), Maria Mubarakshina (b,c), Jochen R. Golecki (a), Giles N. Johnson (d), Anja Krieger-Liszkay (b,*) Abstract: The function of cytochrome b559 (cyt b559) in photosystem II (PSII) was studied in a tobacco mutant in which the conserved phenylalanine at position 26 in the [beta]-subunit was changed to serine. Young leaves of the mutant showed no significant difference in chloroplast ultra structure or in the amount and activity of PSII, while in mature leaves the size of the grana stacks and the amount of PSII were significantly reduced. Mature leaves of the mutant showed a higher susceptibility to photoinhibition and a higher production of singlet oxygen, as shown by spin trapping electron paramagnetic resonance (EPR) spectroscopy. Oxygen consumption and superoxide production were studied in thylakoid membranes in which the Mn cluster was removed to ensure that all the cyt b559 was present in its low potential form. In thylakoid membranes, from wild-type plants, the larger fraction of superoxide production was 3-(3,4-dichlorophenyl)-1,1-dimethylurea-sensitive. This type of superoxide formation was absent in thylakoid membranes from the mutant. The physiological importance of the plastoquinol oxidation by cyt b559 for photosynthesis is discussed. Author Affiliation: (a)Institut fur Biologie II , Universitat Freiburg, Schanzlestr. 1, 79104 Freiburg, Germany (b)CEA, iBiTecS, CNRS URA 2096, Service de Bioenergetique Biologie Structurale et Mecanisme, 91191 Gif-sur-Yvette Cedex, France (c)Institute of Basic Biological Problems RAS, 142290 Pushchino, Moscow region, Russia (d)Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK Article History: Received 29 June 2009; revised 10 October 2009 Article note: (*) e-mail: anja.krieger-liszkay@cea.fr
    Keywords: Active Oxygen ; Plant Biochemistry ; Phenylalanine ; Photosynthesis ; Oxidases ; Superoxides
    ISSN: 0031-9317
    Source: Cengage Learning, Inc.
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
  • 3
    Article
    Article
    Putative function of cytochrome b559 as a plastoquinol oxidase.(Report) (2010)
    Details
    Language: English
    In: Physiologia Plantarum, April, 2010, Vol.138, p.463(11)
    Description: To authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1111/j.1399-3054.2009.01312.x Byline: Natallia Bondarava (a), Christine M. Gross (b), Maria Mubarakshina (b,c), Jochen R. Golecki (a), Giles N. Johnson (d), Anja Krieger-Liszkay (b,*) Abstract: The function of cytochrome b559 (cyt b559) in photosystem II (PSII) was studied in a tobacco mutant in which the conserved phenylalanine at position 26 in the [beta]-subunit was changed to serine. Young leaves of the mutant showed no significant difference in chloroplast ultra structure or in the amount and activity of PSII, while in mature leaves the size of the grana stacks and the amount of PSII were significantly reduced. Mature leaves of the mutant showed a higher susceptibility to photoinhibition and a higher production of singlet oxygen, as shown by spin trapping electron paramagnetic resonance (EPR) spectroscopy. Oxygen consumption and superoxide production were studied in thylakoid membranes in which the Mn cluster was removed to ensure that all the cyt b559 was present in its low potential form. In thylakoid membranes, from wild-type plants, the larger fraction of superoxide production was 3-(3,4-dichlorophenyl)-1,1-dimethylurea-sensitive. This type of superoxide formation was absent in thylakoid membranes from the mutant. The physiological importance of the plastoquinol oxidation by cyt b559 for photosynthesis is discussed. Author Affiliation: (a)Institut fur Biologie II , Universitat Freiburg, Schanzlestr. 1, 79104 Freiburg, Germany (b)CEA, iBiTecS, CNRS URA 2096, Service de Bioenergetique Biologie Structurale et Mecanisme, 91191 Gif-sur-Yvette Cedex, France (c)Institute of Basic Biological Problems RAS, 142290 Pushchino, Moscow region, Russia (d)Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK Article History: Received 29 June 2009; revised 10 October 2009 Article note: (*) e-mail: anja.krieger-liszkay@cea.fr
    Keywords: Active Oxygen ; Plant Biochemistry ; Phenylalanine ; Photosynthesis ; Oxidases ; Superoxides
    ISSN: 0031-9317
    Source: Cengage Learning, Inc.
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
  • 4
    Article
    Article
    The chloroplast HSP70B-CDJ2-CGE1 chaperones catalyse assembly and disassembly of VIPP1 oligomers in Chlamydomonas (2007)
    Details
    Language: English
    In: The Plant journal : for cell and molecular biology, April 2007, Vol.50(2), pp.265-77
    Description: The vesicle-inducing protein in plastids (VIPP1) is essential for the biogenesis of thylakoid membranes in cyanobacteria and plants. VIPP1 and its bacterial ancestor PspA form large homo-oligomeric rings of 〉1 MDa. We recently demonstrated that VIPP1 interacts with the chloroplast J-domain co-chaperone CDJ2 and its chaperone partner HSP70B, and hypothesized that the chaperones might be involved in the assembly and/or disassembly of VIPP1 oligomers. To test this hypothesis, we analysed the composition of VIPP1/chaperone complexes in Chlamydomonas reinhardtii cell extracts and monitored effects of the chaperones on VIPP1 assembly states in vitro. We found that CGE1, the chloroplast GrpE homologue, is also part of complexes with HSP70B, CDJ2 and VIPP1. We observed that CDJ2-VIPP1 accumulated as low- and high-molecular-weight complexes in ATP-depleted cell extracts, but as intermediate-size complexes in extracts supplemented with ATP. This was consistent with a role for the chaperones in VIPP1 assembly and disassembly. Using purified proteins, we could demonstrate that the chaperones indeed facilitated both the assembly and disassembly of VIPP1 oligomers. Electron microscopy studies revealed that, in contrast to PspA, VIPP1 rings assembled into rod-shaped supercomplexes that were morphologically similar to microtubule-like structures observed earlier in various plastid types. VIPP1 rods, too, were disassembled by the chaperones, and chaperone-mediated rod disassembly also occurred when VIPP1 lacked an approximately 30-aa C-terminal extension present in VIPP1 homologues but absent in PspA. By regulating the assembly state of VIPP1, the chloroplast HSP70 chaperone system may play an important role in the maintenance/biogenesis of thylakoid membranes.
    Keywords: Bacterial Proteins -- Metabolism ; Chlamydomonas Reinhardtii -- Metabolism ; Chloroplasts -- Metabolism ; Hsp70 Heat-Shock Proteins -- Metabolism ; Membrane Proteins -- Metabolism ; Molecular Chaperones -- Metabolism
    ISSN: 0960-7412
    E-ISSN: 1365313X
    DOI: 10.1111/j.1365-313X.2007.03047.x
    URL: View this record in MEDLINE/PubMed
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
    Open Access Request
  • 5
    Article
    Article
    Putative function of cytochrome b559 as a plastoquinol oxidase (2010)
    Details
    In: Physiologia Plantarum, April 2010, Vol.138(4), pp.463-473
    Description: The function of cytochrome b559 (cyt b559) in photosystem II (PSII) was studied in a tobacco mutant in which the conserved phenylalanine at position 26 in the β‐subunit was changed to serine. Young leaves of the mutant showed no significant difference in chloroplast ultra structure or in the amount and activity of PSII, while in mature leaves the size of the grana stacks and the amount of PSII were significantly reduced. Mature leaves of the mutant showed a higher susceptibility to photoinhibition and a higher production of singlet oxygen, as shown by spin trapping electron paramagnetic resonance (EPR) spectroscopy. Oxygen consumption and superoxide production were studied in thylakoid membranes in which the Mn cluster was removed to ensure that all the cyt b559 was present in its low potential form. In thylakoid membranes, from wild‐type plants, the larger fraction of superoxide production was 3‐(3,4‐dichlorophenyl)‐1,1‐dimethylurea‐sensitive. This type of superoxide formation was absent in thylakoid membranes from the mutant. The physiological importance of the plastoquinol oxidation by cyt b559 for photosynthesis is discussed.
    Keywords: Cytochrome B Group -- Metabolism ; Oxidoreductases -- Metabolism ; Photosystem II Protein Complex -- Metabolism ; Plastoquinone -- Analogs & Derivatives;
    ISSN: 0031-9317
    E-ISSN: 1399-3054
    DOI: 10.1111/j.1399-3054.2009.01312.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
    Open Access Request
  • 6
    Article
    Article
    Magnetic-field-induced orientation of photosynthetic reaction centers, as revealed by time-resolved D-band electron paramagnetic resonance of spin-correlated radical pairs. II. field dependence of the alignment (2004)
    Details
    Language: English
    In: Journal of Physical Chemistry B, July 8, 2004, Vol.108(27), p.9498(7)
    Description: Time resolved D-band (130 GHz) electron paramagnetic resonance (EPR) has been used to study magnetic-field-induced orientation of photosynthetic reaction centers. This indicates that whole cells are aligned in the magneto-orientation process.
    Keywords: Electron Paramagnetic Resonance -- Usage ; Spin Labeling -- Research ; Magnetic Fields -- Research ; Physical Chemistry -- Research
    ISSN: 1520-6106
    ISSN: 10895647
    E-ISSN: 15205207
    DOI: 10.1021/jp036232c
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
    Open Access Request
  • 7
    Article
    Article
    Chemisorption of Exchange‐Coupled [Ni 2 L(dppba)] + Complexes on Gold by Using Ambidentate 4‐(Diphenylphosphino)benzoate Co‐Ligands (2013)
    Details
    Language: English
    In: Chemistry – A European Journal, 10 June 2013, Vol.19(24), pp.7787-7801
    Description: A new strategy for the fixation of redox‐active dinickel(II) complexes with high‐spin ground states to gold surfaces was developed. The dinickel(II) complex [NiL(Cl)]ClO (ClO), in which L represents a 24‐membered macrocyclic hexaaza‐dithiophenolate ligand, reacts with ambidentate 4‐(diphenylphosphino)benzoate (dppba) to form the carboxylato‐bridged complex [NiL(dppba)], which can be isolated as an air‐stable perchlorate [NiL(dppba)]ClO (ClO) or tetraphenylborate [NiL(dppba)]BPh (BPh) salt. The auration of ClO was probed on a molecular level, by reaction with AuCl, which leads to the monoaurated NiAu complex [NiL(dppba)AuCl]ClO (ClO). Metathesis of ClO with NaBPh produces [NiL(dppba)AuPh]BPh (BPh), in which the Cl is replaced by a Ph group. The complexes were fully characterized by ESI mass spectrometry, IR and UV/Vis spectroscopy, X‐ray crystallography (BPh and BPh), cyclic voltammetry, SQUID magnetometry and HF‐ESR spectroscopy. Temperature‐dependent magnetic susceptibility measurements reveal a ferromagnetic coupling =+15.9 and +17.9 cm between the two Ni ions in ClO and BPh (H=−2 SS). HF‐ESR measurements yield a negative axial magnetic anisotropy (〈0), which implies a bistable (easy axis) magnetic ground state. The binding of the [NiL(dppba)]ClO complex to gold was ascertained by four complementary surface analytical methods: contact angle measurements, atomic‐force microscopy, X‐ray photoelectron spectroscopy, and spectroscopic ellipsometry. The results indicate that the complexes are attached to the Au surface through coordinative AuP bonds in a monolayer. : The chemisorption of exchange‐coupled [NiL(OCHPPh)] complexes on gold through the ambidentate 4‐(diphenylphosphino)benzoate co‐ligand is reported (see figure). The binding of the macrocyclic Ni complexes was studied by water contact angle measurements, atomic‐force microscopy, X‐ray photoelectron spectroscopy, and ellipsometry, by using a discrete trinuclear NiAu complex [NiL(OCCHPPh)AuPPh] as a spectroscopic and structural probe.
    Keywords: Chemisorption ; Gold ; Ligands ; Macrocyclic Ligands ; Nickel ; Phosphorus Heterocycles
    ISSN: 0947-6539
    E-ISSN: 1521-3765
    DOI: 10.1002/chem.201300496
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
    Open Access Request
  • 8
    Article
    Article
    Evidence that cytochrome b559 mediates the oxidation of reduced plastoquinone in the dark (2003)
    Details
    Language: English
    In: The Journal of biological chemistry, 11 April 2003, Vol.278(15), pp.13554-60
    Description: The function of cytochrome b(559) in photosystem II (PSII) was investigated using a mutant created in tobacco in which the conserved phenylalanine at position 26 in the beta-subunit (PsbF) was changed to serine (Bock, R., Kössel, H., and Maliga, P. (1994) EMBO J. 13, 4623-4628). The mutant grew photoautotrophically, but the amount of PSII was reduced and the ultrastructure of the chloroplast was dramatically altered. Very few grana stacks were formed in the mutant. Although isolated PSII-enriched membrane fragments showed low PSII activity, electron paramagnetic resonance indicated the presence of functional PSII. Difference absorption spectra showed that the cytochrome b(559) contained heme. The plastoquinone pool was largely reduced in dark-adapted leaves of the mutant, based on chlorophyll fluorescence and thermoluminescence measurements. We therefore propose that cytochrome b(559) plays an important role in PSII by keeping the plastoquinone pool and thereby the acceptor side of PSII oxidized in the dark. Structural alterations as induced by the single Phe --〉 Ser point mutation in the transmembrane domain of PsbF evidently inhibit this function.
    Keywords: Photosystem II Protein Complex ; Chlorophyll -- Metabolism ; Cytochrome B Group -- Metabolism ; Plastoquinone -- Metabolism ; Tobacco -- Metabolism
    ISSN: 0021-9258
    E-ISSN: 1083351X
    DOI: 10.1074/jbc.M212842200
    URL: View this record in MEDLINE/PubMed
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
    Open Access Request
  • 9
    Article
    Article
    VIPP1 oligomer assembly/disassembly (2007)
    Details
    Language: English
    In: Plant journal for cell and molecular biology, 2007, Vol.50(2), pp.265-277
    Description: The vesicle-inducing protein in plastids (VIPP1) is essential for the biogenesis of thylakoid membranes in cyanobacteria and plants. VIPP1 and its bacterial ancestor PspA form large homo-oligomeric rings of 〉1 MDa. We recently demonstrated that VIPP1 interacts with the chloroplast J-domain co-chaperone CDJ2 and its chaperone partner HSP70B, and hypothesized that the chaperones might be involved in the assembly and/or disassembly of VIPP1 oligomers. To test this hypothesis, we analysed the composition of VIPP1/chaperone complexes in Chlamydomonas reinhardtii cell extracts and monitored effects of the chaperones on VIPP1 assembly states in vitro. We found that CGE1, the chloroplast GrpE homologue, is also part of complexes with HSP70B, CDJ2 and VIPP1. We observed that CDJ2-VIPP1 accumulated as low- and high-molecular-weight complexes in ATP-depleted cell extracts, but as intermediate-size complexes in extracts supplemented with ATP. This was consistent with a role for the chaperones in VIPP1 assembly and disassembly. Using purified proteins, we could demonstrate that the chaperones indeed facilitated both the assembly and disassembly of VIPP1 oligomers. Electron microscopy studies revealed that, in contrast to PspA, VIPP1 rings assembled into rod-shaped supercomplexes that were morphologically similar to microtubule-like structures observed earlier in various plastid types. VIPP1 rods, too, were disassembled by the chaperones, and chaperone-mediated rod disassembly also occurred when VIPP1 lacked an approximately 30-aa C-terminal extension present in VIPP1 homologues but absent in PspA. By regulating the assembly state of VIPP1, the chloroplast HSP70 chaperone system may play an important role in the maintenance/biogenesis of thylakoid membranes. ; Includes references ; p. 265-277.
    Keywords: Thylakoid Biogenesis ; J-Domain Protein ; Chloroplast Chaperone Function ; Grpe; Microtubule-Like Structures ; Protein Complex Assembly And Disassembly
    ISSN: 0960-7412
    Source: AGRIS (Food and Agriculture Organization of the United Nations)
    URL: View full text (authentication may be required)
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
  • 10
    Article
    Article
    The chloroplast HSP70B‐CDJ2‐CGE1 chaperones catalyse assembly and disassembly of VIPP1 oligomers in Chlamydomonas (2007)
    Details
    Language: English
    In: Plant Journal, April 2007, Vol.50(2), pp.265-277
    Description: The vesicle‐inducing protein in plastids (VIPP1) is essential for the biogenesis of thylakoid membranes in cyanobacteria and plants. VIPP1 and its bacterial ancestor PspA form large homo‐oligomeric rings of 〉1 MDa. We recently demonstrated that VIPP1 interacts with the chloroplast J‐domain co‐chaperone CDJ2 and its chaperone partner HSP70B, and hypothesized that the chaperones might be involved in the assembly and/or disassembly of VIPP1 oligomers. To test this hypothesis, we analysed the composition of VIPP1/chaperone complexes in cell extracts and monitored effects of the chaperones on VIPP1 assembly states . We found that CGE1, the chloroplast GrpE homologue, is also part of complexes with HSP70B, CDJ2 and VIPP1. We observed that CDJ2‐VIPP1 accumulated as low‐ and high‐molecular‐weight complexes in ATP‐depleted cell extracts, but as intermediate‐size complexes in extracts supplemented with ATP. This was consistent with a role for the chaperones in VIPP1 assembly and disassembly. Using purified proteins, we could demonstrate that the chaperones indeed facilitated both the assembly and disassembly of VIPP1 oligomers. Electron microscopy studies revealed that, in contrast to PspA, VIPP1 rings assembled into rod‐shaped supercomplexes that were morphologically similar to microtubule‐like structures observed earlier in various plastid types. VIPP1 rods, too, were disassembled by the chaperones, and chaperone‐mediated rod disassembly also occurred when VIPP1 lacked an approximately 30‐aa C‐terminal extension present in VIPP1 homologues but absent in PspA. By regulating the assembly state of VIPP1, the chloroplast HSP70 chaperone system may play an important role in the maintenance/biogenesis of thylakoid membranes.
    Keywords: Chloroplast Chaperone Function ; Thylakoid Biogenesis ; Protein Complex Assembly And Disassembly ; J‐Domain Protein ; Grpe; Microtubule‐Like Structures
    ISSN: 0960-7412
    E-ISSN: 1365-313X
    DOI: 10.1111/j.1365-313X.2007.03047.x
    Source: John Wiley & Sons, Inc.
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Article
    Open Access Request
Nothing or not found what you are looking for? Please check your search query or use the Interlibrary Loan Search.
Close ⊗
This website uses cookies and the analysis tool Matomo. Further information can be found on the KOBV privacy pages