Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts

Waegemann, Karin; Soll, Jürgen

doi:10.1046/j.1365-313x.1991.00149.x

Cited by 83 publications

(163 citation statements)

References 9 publications

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“…Productive binding of the precursor to the receptor requires ATP hydrolysis. ATP concentrations between 1-100 μΜ have been determined to support binding to isolated organelles (8), right-side-out envelope vesicles (29) and the isolated import apparatus (30).…”

Section: Binding Of Precursor Proteins To the Organellar Surfacementioning

confidence: 99%

“…Recently it was demonstrated that it is possible to isolate a membrane complex loaded with pSSU from purified outer chloroplast envelopes (29,30). After incubation with pSSU translation product and reisolation the outer envelope vesicles were solubilized by digitonin and subjected to fractionation on a linear sucrose gradient.…”

Section: Components Of the Translocation Apparatusmentioning

confidence: 99%

“…Additionally the isolated import complex (29) and the outer envelope membranes (27, 51) do contain hsc 70 homologues which could play a role in the translocation event. Von Heijne and Nishikawa (52) propose that chloroplast transit peptides are essentially devoid of regular secondary or tertiary motifs and that such unfolded structures are favorable for guidance of chaperones operating at different steps of the chloroplast protein import pathway.…”

Section: Components Of the Translocation Apparatusmentioning

confidence: 99%

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Protein import into chloroplasts

Soll

2002

Current Opinion in Plant Biology

186

241

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Section: Binding Of Precursor Proteins To the Organellar Surfacementioning

confidence: 99%

Section: Components Of the Translocation Apparatusmentioning

confidence: 99%

Section: Components Of the Translocation Apparatusmentioning

confidence: 99%

See 1 more Smart Citation

Protein import into chloroplasts

Soll

2002

Current Opinion in Plant Biology

186

241

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“…Furthermore translocation intermediates detected in intact chloroplasts were also found in this import complex after protease treatment. This indicated that not only a functionally active receptor but that also part of the translocation apparatus was retained actively in this isolated membraneprotein complex (8,20). Furthermore preSSU can be crosslinked to OEP75 in the isolated complex by CuCl2 (Fig.…”

Section: A)mentioning

confidence: 81%

The Protein Import Machinery of Chloroplasts

Soll¹,

Seedorf²

1995

Photosynthesis: From Light to Biosphere

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“…Purified chloroplasts were isolated from 12-day-old pea plants by standard procedures [23]. The chloroplasts equiv, to 5 mg chlorophyll were lysed in 75 ml 50 mM NaPi-buffer pH 7.4, 10 mM NaC1.…”

Section: Isolation and Jractionation Of Chloroplastsmentioning

confidence: 99%

Molecular chaperones are present in the thylakoid lumen of pea chloroplasts

Schlicher

Soll

1996

FEBS Letters

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A soluble protein fraction was obtained from pea chloroplast thylakoids, which represents highly enriched lumenal components. Using antisera against chaperonin 60 (cpn60), chaperonin 10 (cpnl0) and the heat shock cognate protein of 70 kDa (hsc70) we are able to demonstrate, that the thylakoid lumen contains a separate set of molecular chaperones, which is distinct from the stromal one. In contrast to the a and ~ subunits of cpn60 present in the stroma the lumen contains only one cpn60 isoform of distinct isoelectric point. Furthermore the lumenal cpnl0 is of 'normal' size and not like its stromal counterpart of a doubledomain tandem architecture. The immunoreactive hsc70 isoforms in the lumen seem also to be different from the stromal ones. Thus, chloroplasts seem to contain the largest number of molecular chaperone isoforms present in one organelle.Key words'." Pisum sativum L.; Chaperone; Thylakoid lumen; Protein assembly stromal proteins can be folded by heterologous non chloroplast cpn60/cpnl0 systems [16,17].The thylakoid lumen houses a number of proteins, of which most prominent are the nuclear encoded components of the oxygen evolving enzyme complex (OEE) associated with photosystem II and also plastocyanin, a mobil electroncarrier between the cytochrome b/f complex and photosystem I [2]. Following thylakoid transfer the OEE subunits must be assembled into the functional complex. We thus wanted to know, if this chloroplast subcompartment contained the molecular chaperones necessary for folding and assembly. Our data demonstrate that the thylakoid lumen contains a 'normal' cpn60/cpn 10 system distinct from the unusual stromal system and novel hsc70 homologues. The coexistence of two chaperonin systems in one organelle could have provoked the differential development (evolution) of its components. Materials and methods

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Characterization of the protein import apparatus in isolated outer envelopes of chloroplasts

Cited by 83 publications

References 9 publications

Protein import into chloroplasts

Protein import into chloroplasts

The Protein Import Machinery of Chloroplasts

Molecular chaperones are present in the thylakoid lumen of pea chloroplasts

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