Transport of proteins into mitochondria and chloroplasts.

Chua, Nam‐Hai; Schmidt, Gregory W.

doi:10.1083/jcb.81.3.461

Cited by 339 publications

(136 citation statements)

References 38 publications

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“…The majority of proteins within mitochondria and chloroplasts, for example, are coded for by nuclear genes and are synthesized on cytoplasmic polyribosomes (35,193). For several such proteins it has been shown that incorporation into the organelle occurs posttranslationally and, therefore, free polypeptides must in some way pass through the limiting membranes (34,82,84,91,128,129,165).…”

Section: Posttranslational Transfer Of Polypeptides To Their Sites Ofmentioning

confidence: 99%

Mechanisms for the incorporation of proteins in membranes and organelles.

Sabatini¹,

Kreibich²,

Morimoto³

et al. 1982

The Journal of Cell Biology

869

281

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Section: Posttranslational Transfer Of Polypeptides To Their Sites Ofmentioning

confidence: 99%

Mechanisms for the incorporation of proteins in membranes and organelles.

Sabatini¹,

Kreibich²,

Morimoto³

et al. 1982

The Journal of Cell Biology

869

281

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“…(b) Binding is specific for precursor forms of plastid proteins [179]; when mature proteins are used for uptake, they do not bind to isolated chloroplasts and are not transported either [180].…”

Section: Precursor Binding To the Outer Envelope Membranementioning

confidence: 99%

Molecular aspects of plastid envelope biochemistry

Joyard

Block

Douce

1991

European Journal of Biochemistry

118

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“…It should be noted that e.g. the small subunit of ribulose bisphosphate carboxylase is formed from a precursor with higher molecular weight than the native protein, which is also reactive with an antibody formed against the small subunit of the enzyme [22,23].…”

Section: Discussionmentioning

confidence: 99%

High Variability of the Electron Carrier Plastocyanin in Microalgae

Bohner¹,

Merkle²,

Kroneck³

et al. 1980

European Journal of Biochemistry

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The plastocyanin content of Scenedesmus can be dramatically varied with the copper content of the culture medium. Figures as high as 7 mmol plastocyanin/mol chlorophyll are possible. Electron paramagnetic resonance (EPR) spectroscopy has been used to determine this physiological response quantitatively in intact cells having different amounts of plastocyanin. The results obtained by the EPR technique were compared with data on isolated plastocyanin determined either by spectro‐photometry or immunoelectrophoresis. Agreement was found for the amount of plastocyanin detected by the first two methods, whereas the last assay yielded data at least 25% higher on the average. Under all culture conditions a copper‐free plastocyanin precursor is present. The EPR properties of purified plastocyanin and those of cellular plastocyanin located within the thylakoids are practically identical in terms of g‐values, hyperfine splittings, signal linewidths and saturation behavior at temperatures of 12‐15 K. Our data indicate that plastocyanin is not present in a membrane‐bound form but exists as a single soluble pool. The studies have been extended to the algae Dunaliella parva and Bumilleriopsis filiformis. The first species exhibits a limited variation of plastocyanin with the copper content of the medium. Furthermore, no cytochrome c‐553 could be detected in Dunaliella even under conditions of copper deficiency. In contrast, Bumilleriopsis does not contain plastocyanin regardiess of the amount of copper offered.

show abstract

Transport of proteins into mitochondria and chloroplasts.

Cited by 339 publications

References 38 publications

Mechanisms for the incorporation of proteins in membranes and organelles.

Mechanisms for the incorporation of proteins in membranes and organelles.

Molecular aspects of plastid envelope biochemistry

High Variability of the Electron Carrier Plastocyanin in Microalgae

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