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'Q B Protein' in keywords
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1987 (1)
1984 (2)
1Author    N. Pucheu, G.F W IldnerRequires cookie*
 Title    Isolation of 3 2 -3 5 kDa Thylakoid Proteins from Chlamydomonas reinhardii  
 Abstract    The protein com position o f Chlamydomonas reinhardii thylakoids in the m olecular weight range o f 3 2 -3 5 kDa was studied. The thylakoids were labelled with 32P —Pj in vivo using Pr starved cell cultures, solubilized with SDS and separated by polyacrylam ide gradient gel electrophoresis. The following differentiation o f proteins could be accom plished: two proteins were phosphorylated, which were also well stained with C oom assie blue, and one major protein was only detected by the silver staining procedure. The m obility o f the latter protein is different in gels with urea, showing an apparently lower molecular weight. In order to investigate whether a functional photosystem II is obligatory for protein phos­ phorylation, the phosphorylation o f thylakoid proteins was studied with a photosystem II deficient mutant. The mutant, which had normal photosystem I activity, but lacked photo­ system II activity, could synthesize ATP light dependently; its m ain labelled protein bands had a molecular weight o f 3 2 -3 5 kDa; it contained the light harvesting protein chlorophyll com plex and an unknown protein at 22 kDa. The 32P incorporation in photosystem II deficient cells was comparable to cells with functional photosystem II units. 
  Reference    Z. Naturforsch. 39c, 434 (1984); received N ovem ber 30 1983 
  Published    1984 
  Keywords    Photosystem II Complex, Q B-Protein, Chlamydomonas reinhardii, Protein Phosphorylation, Photosystem II Deficiency 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0434.pdf 
 Identifier    ZNC-1984-39c-0434 
 Volume    39 
2Author    N. Pucheu, W. Oettmeier, U. H. Eisterkam, K. Masson, G.F W IldnerRequires cookie*
 Title    Metribuzin-Resistant Mutants of Chlamydomonas reinhardii  
 Abstract    Herbicide resistance in Chlamydomonas reinhardii cells was induced by m utagenesis with 5-fluorodeoxyuridine and ethylm ethanesulfonate. Four m utant strains were isolated and analyzed for resistance against D C M U -type or phenolic inhibitors o f photosynthetic electron transport. The mutants were different in both the extent and the pattern o f their resistance: the R / S value, i.e. the ratio o f / 50 values o f the inhibition o f photosynthetic electron transport in isolated resistant and susceptible thylakoids, varied for m etribuzin from 10 000 to 36. The mutant MZ-1 was resistant against metribuzin, atrazine and D C M U , whereas the mutant M Z-2 showed resistance mainly against metribuzin and atrazine. The m utant M Z-3 was sim ilar to MZ-1, but showed a lesser extent o f resistance against D C M U . The m utant M Z-4 show ed resistance against metribuzin, but not against atrazine. These results dem onstrate that the resistance against one herbicide o f the D C M U -type (m etribuzin) must not be accom panied by sim ilar resistance against te other inhibitors. Binding studies with radioactively labeled herbicides, [l4C]metribuzin, [HC]atrazine and [3H]DCM U, and isolated thylakoids supported these observations. Phosphorylation o f thylakoid m embrane proteins was studied with w ild-type cells and resistant mutants under in vivo conditions in the light. The 32P-labeled m ain proteins bands were in the molecular weight range o f 1 0 -1 4 kDa, 2 6 -2 9 kD a, 3 2 -3 5 kD a and 4 6 -4 8 kDa. The pattern and the extent o f incorporation o f 32P were sim ilar for the m utants and the w ild-type cells. 
  Reference    Z. Naturforsch. 39c, 437—439 (1984); received N ovem ber 30 1983 
  Published    1984 
  Keywords    Metribuzin, Chlamydomonas reinhardii, Q B-Protein, H erbicide R esistance, Thylakoid Phosphorylation 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0437.pdf 
 Identifier    ZNC-1984-39c-0437 
 Volume    39 
3Author    G. Ünter, F. W. Ildner, Claudia Fiebig, N. Orbert Dedner, H. E. MeyerRequires cookie*
 Title    The Use of HPLC for the Purification of the QB-Protein  
 Abstract    The 0 B-protein is as a hydrophobic integral membrane protein firmly bound in the reaction center com plex o f photosystem II. A new method was developed to purify the SD S extracted protein using reversed-phase chromatography with two binary linear gradient systems. The iden­ tification o f the 0 B-protein was achieved by its rapidly labeling during photoassim ilation of [35S]sulfate and by its reaction with the photoaffinity label azido-[14C]atrazine. Furtherm ore, antisera against the purified Q B-protein reacted with a single peak fraction, the second peak o f the chrom atogram , which was identical with the labeled protein peak fraction. 
  Reference    Z. Naturforsch. 42c, 739 (1987); received N ovem ber 10 1986 
  Published    1987 
  Keywords    H PLC-Protein Purification, Q B-Protein, D -l Protein, psbA G ene, Chlamydomonas reinhardii 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0739.pdf 
 Identifier    ZNC-1987-42c-0739 
 Volume    42