Transverse organization of components within the chloroplast cytochrome b-563f complex

Mansfield, Royston W.; Anderson, Jan M.

doi:10.1016/0005-2728(85)90195-1

Cited by 29 publications

(10 citation statements)

References 22 publications

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“…The orientation of the cytochrome b-563 and subunit IV polypeptides in the thylakoid membrane has been investigated by proteolytic digestion of inside-out and right-side-out vesicles of pea chloroplast membranes (Mansfield and Anderson 1985). These experiments indicated that the C-termini of both polypeptides were accessible to carboxypeptidase digestion in right-side-out vesicles.…”

Section: Membrane Topology Of Components Of the Cytochrome B-f Commentioning

confidence: 99%

Synthesis and assembly of the cytochrome b-f complex in higher plants

Willey

Gray

1988

Photosynth Res

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The cytochrome b-f complex is composed of four polypeptide subunits, three of which, cytochrome f, cytochrome b-563 and subunit IV, are encoded in chloroplast DNA and synthesised within the chloroplast, and the fourth, the Rieske FeS protein, is encoded in nuclear DNA and synthesised in the cytoplasm. The assembly of the cytochrome b-f complex therefore requires the interaction of subunits encoded by different genomes. A key role for the nuclear-encoded Rieske FeS protein in the assembly of the complex is suggested by a study of cytochrome b-f complex mutants. The assembly of individual subunits of the complex may be regulated by the availability of prosthetic groups. The genes for the chloroplast-encoded subunits and cDNA clones for the Rieske FeS protein have been isolated and characterised. Cytochrome f and the Rieske FeS protein are synthesised initially with N-terminal presequences required for their correct assembly within the chloroplast. The deduced amino acid sequences of the four subunits have been used to suggest models for the arrangement of the polypeptides in the thylakoid membrane.

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Section: Membrane Topology Of Components Of the Cytochrome B-f Commentioning

confidence: 99%

Synthesis and assembly of the cytochrome b-f complex in higher plants

Willey

Gray

1988

Photosynth Res

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“…It has been speculated that the ten highly conserved basic amino acids give rise to a positively charged region between residues 58 to 154, which may be important for binding plastocyanin the oxidant of cytochrome f . Evidence that most of the protein is exposed at the inner surface and that the haem is located in this region has come from proteolytic digestion and immunological studies with isolated thylakoid membranes Mansfield and Bendall, 1984;Mansfield and Anderson, 1985).…”

Section: Cytochrome Fmentioning

confidence: 99%

Photosynthesis and the Application of Molecular Genetics

Barber

Marder

1986

Biotechnology and Genetic Engineering Reviews

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“…terminus of the cytochrome f polypeptide is located at the stromal membrane surface (28,29), whereas the NH2 and COOH termini of the b559 polypeptide are located at the stromal and lumenal surfaces, respectively (30). Treatment of intact (or right-side-out) thylakoids with carboxypeptidase, but not with trypsin, removes a 1-kDa region of the cyhylakoid memtochromefpolypeptide (ref.…”

mentioning

confidence: 99%

“…Secondly, subunit 5 shares the structural anomaly of a membrane-embedded proline (Pro-15) (33) with several of the hydrophobic regions of the cytochrome b6 polypeptide; others have speculated on the role of embedded prolines in conformational changes linked to cross-membrane proton transport (34). The COOH terminus of subunit 5 is located at the stromal membrane surface, an orientation shared with all four previously characterized b6-f polypeptides (28,29). A role for the subunit 5 polypeptide might be established by determining the effect(s) of anti-sp37 serum binding to the COOH terminus on functions ofthe complex-such as proton…”

mentioning

confidence: 99%

A 4-kDa maize chloroplast polypeptide associated with the cytochrome b6-f complex: subunit 5, encoded by the chloroplast petE gene.

Haley

Bogorad

1989

Proc. Natl. Acad. Sci. U.S.A.

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Four polypeptides, three of which are chloroplast-encoded, have been shown to be associated with the thylakoid membrane cytochrome b6-f complex. In this report, the gene for a fifth polypeptide, which copurifies with the b6-f complex, is identified through the use of an antibody generated against a synthetic decapeptide predicted from a maize chloroplast DNA sequence. The deduced 37-amino acid sequence ofthe immunoreactive 4-kDa polypeptide is 100% and 86% conserved in the respective similar open reading frames encoded by Nicotiana tabacum and Marchanta chloroplast DNA. The 4-kDa polypeptide is present in both etioplasts and chloroplasts of maize and is found as well in spinach, tobacco, pea, wheat, and rice thylakoids. Similar to the other subunits ofthe bG-fcomplex, it is intrinsic to the membrane, and its hydrophilic COOH terminus is located at the stromal thylakoid surface. We propose to call the 4-kDa polypeptide "subunit 5" and the chloroplast gene that encodes it the petE gene.

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Transverse organization of components within the chloroplast cytochrome b-563f complex

Cited by 29 publications

References 22 publications

Synthesis and assembly of the cytochrome b-f complex in higher plants

Synthesis and assembly of the cytochrome b-f complex in higher plants

Photosynthesis and the Application of Molecular Genetics

A 4-kDa maize chloroplast polypeptide associated with the cytochrome b6-f complex: subunit 5, encoded by the chloroplast petE gene.

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