Purification of cytochrome b-559 from oxygen-evolving Photosystem II preparations of spinach and maize

Metz, James G.; Ulmer, Gregory L.; Bricker, Terry M.; Miles, Donald

doi:10.1016/0005-2728(83)90240-2

Cited by 30 publications

(14 citation statements)

References 19 publications

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“…A similar M value for the cytoc~rome was obtained starting with PSII particles f~om maize (19). The gels also showed other minor bands, particularly one near M 8,000 and a weakly staining M 6,000 band.…”

Section: (18)supporting

confidence: 52%

“…Regarding structure, recent advances in understanding of the amino acid composition, heme coordination, nucleotlde and amino acid sequence, and polypeptide composition of cytochrome h-559 have relied on a combination of biochemical, biophysical, and molecular biologlcal approaches (3,4,(18)(19)(20). These data have led to conclusions concerning the arrangement of the cytochrome in the membrane ( The initial step in the purification, the extraction of membranes with 2% Triton X-100 and 4 M urea, was developed by Wasserman and coworkers (22,23), who reported that the purified cytochrome was made of small electrophoretlcally similar subunits of M r 5,600 with three [248] different NH2-termini , in a complex oligomeric (octamerlc) lipoprotein of II0,000 molecular weight.…”

Section: Introductionmentioning

confidence: 99%

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On the structure and function of cytochrome b-559

1986

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A sumary of biochemical, biophysical, and molecular biological data is presented which led to the identification of two different polypeptides (α and β, MW=9.16 and 4.27 kDa) in the cytochrome b-559 protein. The presence of a single His residue on each polypeptide, and the conclusion from spectroscopy that the heme coordination must be bis-histidine led to an obligatory requirement for coordination of a single heme through a heme cross-linked dimer. This structure does not have a precedent among soluble or membrane bound cytochromes. The possible participation of the cytochrome in the pathway of photoactivation is discussed.

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Section: (18)supporting

confidence: 52%

Section: Introductionmentioning

confidence: 99%

On the structure and function of cytochrome b-559

1986

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“…The Table 2 Comparison of (A) NHz-terminal amino acid sequence of the isolated small polypeptide and (B) the sequence predicted for the 4.27 kDa product of the downstream reading frame The actual M, of the band originally described as A4, 6000 is 4268 without the N-terminal methionine [4]. The ubiquitous presence of this low-M, band in gels of cytochrome b-5.59 purified from PS II particles of maize had been noted [2]. Not only is the 4.27 kDa downstream gene product present in gels containing cytochrome 6-559 from spinach thylakoid membranes [l], but the stoichiometry of this component is approx.…”

Section: Resultsmentioning

confidence: 99%

“…The purification of a small 9 kDa polypeptide [1,2] indicated that the structure of this protein might be relatively simple. More recent data suggested a more complicated structure , and the studies discussed here document that the cytochrome contains a second smaller polypeptide.…”

Section: Introductionmentioning

confidence: 99%

Evidence for a hetero‐oligomeric structure of the chloroplast cytochrome b‐559

1985

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A second nonhomologous polypeptide in the thylakoid membrane cytochrome b‐559 has been suggested by the finding of a smaller reading frame just slightly downstream from that corresponding to the 9 kDa cytochrome polypeptide that is dominant on a Coomassie‐stained gel. This reading frame encoded a 39‐residue polypeptide that was similar in having a central hydrophobic domain of 25–26 residues and a single His residue at the same position in the hydrophobic domain. The smallest polypeptide seen on SDS gels of the cytochrome was isolated by high‐performance liquid chromatography (HPLC). The NH2‐terminal sequence matched that of the downstream gene. The stoichiometry of the 2 gene products separated by HPLC was approx. 1:1, based on the molecular masses of 9.16 and 4.27 kDa calculated from the nucleotide sequence. It is concluded that the cytochrome contains both the 9.16 kDa (α) and 4.27 kDa (β) polypeptides. These data, the single His residue on each polypeptide, and the previous finding of a bis‐histidine coordination, imply that the unit heme binding structure of the cytochrome is a heme cross‐linked dimer. If the cytochrome contains a single heme, the dimer structure would be (αβ). If there are 2 hemes/cytochrome, the more likely structure would be (αβ)2, a tetramer consisting of 2 heme cross‐linked hetero‐dimers.

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“…Metz et al (1983) and Widger et al (1984) identified a 9-10 kDa polypeptide associated with maize and spinach cytochrome b-559. Zielinski and Price (1980) had reported that cytochrome b-559 was a product of chloroplast protein synthesis.…”

Section: Introductionmentioning

confidence: 99%

Nucleotide sequence of the genes encoding cytochrome b-559 from the cyanelle genome of Cyanophora paradoxa

Cantrell

Bryant

1988

Photosynth Res

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Cyanophora paradoxa is a flagellated protozoan which possesses unusual, chloroplast-like organelles referred to as cyanelles. The psbE and psbF genes, which encode the two apoprotein subunits of cytochrome b-559, have been cloned from the cyanelle genome of C. paradoxa. The complete nucleotide sequences of these genes and their flanking sequences were determined by the chain-termination, dideoxy method. The psbE gene is composed of 75 codons and predicts a polypeptide of 8462 Da that is seven to nine residues smaller than most other psbE gene products. The psbF gene consists of 43 codons and predicts a polypeptide of 4761 Da. Two open reading frames, whose sequences are highly conserved among cyanobacteria and numerous higher plants, were located in the nucleotide sequence downstream from the psbF gene. The first open reading frame, denoted psbI, is composed of 39 codons, while the second open reading frame, denoted psbJ, is composed of 41 codons. The predicted amino acid sequences of the psbI and psbJ gene products predict proteins of 5473 and 3973 Da respectively. These proteins are probably integral membrane proteins anchored in the membrane by a single, transmembrane alpha helix. The psbEFIJ genes are probably co-transcribed and constitute an operon as found for other organisms. Each of the four genes is preceded by a polypurine sequence which resembles the consensus ribsosome binding sequences for Escherichia coli.

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Purification of cytochrome b-559 from oxygen-evolving Photosystem II preparations of spinach and maize

Cited by 30 publications

References 19 publications

On the structure and function of cytochrome b-559

On the structure and function of cytochrome b-559

Evidence for a hetero‐oligomeric structure of the chloroplast cytochrome b‐559

Nucleotide sequence of the genes encoding cytochrome b-559 from the cyanelle genome of Cyanophora paradoxa

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