Evidence for Chloroplastic Localization of an Ammonium-Inducible Glutamate Dehydrogenase and Synthesis of Its Subunit from a Cytosolic Precursor-Protein in <i>Chlorella sorokiniana</i>

Prunkard, Donna; Bascomb, Newell F.; Robinson, Ralph W.; Schmidt, Robert R.

doi:10.1104/pp.81.2.349

Cited by 21 publications

(13 citation statements)

References 14 publications

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“…The localization of GDH in higher plant and algal chloroplasts has also been reported (7,19,27). In one study, the subunit-precursor of chloroplastic GDH was shown to be synthesized in the cytosol (19).…”

Section: Discussionmentioning

confidence: 99%

“…In one study, the subunit-precursor of chloroplastic GDH was shown to be synthesized in the cytosol (19). However, studies dealing with nongreen plastids and their enzymatic characteristics have received less attention (28).…”

Section: Discussionmentioning

confidence: 99%

“…In a recent study, GDH was found to be localized exclusively in the chloroplast of Chiamydomonas, and the enzyme was shown to be equally active with NAD and NADP (7). An ammonium inducible NADP-GDH was also reported to be located in the chloroplasts of Chlorella, however, its subunit-precursor was shown to be synthesized in the cytosol ( 19).…”

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confidence: 99%

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A Plastidial Localization and Origin of l-Glutamate Dehydrogenase in a Soybean Cell Culture

Bhadula

Shargool²

1991

Plant Physiol.

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The subcellular distribution of L-glutamate dehydrogenase (GDH, EC 1.4.1.3.) was studied in SB3 soybean (Glycine max) cells using subcellular fractionation techniques. Compounds that inhibit protein synthesis either on 80s or 70s ribosomes were also used to give a preliminary idea of which subcellular fraction is involved in GDH synthesis. It was found that whereas cycloheximide and puromycin considerably reduced the total amount of protein synthesized by the cells, they did not appear to inhibit the synthesis of GDH. In the presence of chloramphenicol, both GDH activity and protein level in the cells were considerably reduced, suggesting that this enzyme was synthesized in organelles and not in the cytosol. Streptomycin, which inhibits plastid protein synthesis, also inhibited synthesis of GDH, indicating that a fraction of GDH activity was plastidial in origin. This is supported by the data on subcellular distribution of the enzyme, which showed that a major fraction of GDH is found in the plastidial fraction, although some activity is found associated with the mitochondrial fraction also. Since a major fraction of GDH activity was found in the plastidial fraction, we studied protein synthesis using isolated plastids and 35S-methionine. Using antibodies raised against purified GDH, we identified a 35S-labeled 41-kilodalton polypeptide synthesized by plastids as GDH.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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A Plastidial Localization and Origin of l-Glutamate Dehydrogenase in a Soybean Cell Culture

Bhadula

Shargool²

1991

Plant Physiol.

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“…NADP+-GDH proteins synthesized in cyto-GDH1 sol, as precursors or as subunits, and then transported into and processed within the chloroplasts have been described in Chlorella sorokiniana (17). …”

Section: Isolation and Purification Of Mitochondria From C Reinhardtiimentioning

confidence: 99%

“…In higher plants, NADH-or NAD(P)H-GDH isozymes have been found in mitochondria and cytosol (11,18), whereas an NADP+-GDH has been located in chloroplasts (18). In Chlorella, a constitutive NAD+-GDH is found in mitochondria, but an ammonium-inducible NADP+-GDH is located in chloroplasts (17). In Caulerpa simpliciuscula, the NADP+-GDH is located in chloroplasts (7), whereas in Euglena gracilis, it has been found in cytosol (3).…”

mentioning

confidence: 99%

Intracellular Localization of Three l-Glutamate Dehydrogenase Isozymes from Chlamydomonas reinhardtii

Moyano

Ramazanov²,

Cárdenas³

et al. 1992

Plant Physiol.

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The intracellular localization of the activity and synthesis of three isozymes of NAD(P)+-glutamate dehydrogenase from the unicellular green alga Chiamydomonas reinhardtii cw-92 has been established. Isozyme activities have been located within mitochondria by using differential centrifugation techniques and discontinuous Percoll gradient separations. Experiments with protein synthesis inhibitors cycloheximide, rifampicin, chloramphenicol, and actinomycin D, under dark and carbon starvation conditions, revealed that synthesis of the three isozymes was likely to occur in cytosol as precursor proteins that are then transported and processed inside the mitochondria.

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Role of Amination and Transamination in Ammonium Incorporation in Chlamydomonas Reinhardtii

Cárdenas¹,

Lain‐Guelbenzu²,

Moyano³

et al. 1990

Inorganic Nitrogen in Plants and Microorganisms

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Evidence for Chloroplastic Localization of an Ammonium-Inducible Glutamate Dehydrogenase and Synthesis of Its Subunit from a Cytosolic Precursor-Protein in Chlorella sorokiniana

Cited by 21 publications

References 14 publications

A Plastidial Localization and Origin of l-Glutamate Dehydrogenase in a Soybean Cell Culture

A Plastidial Localization and Origin of l-Glutamate Dehydrogenase in a Soybean Cell Culture

Intracellular Localization of Three l-Glutamate Dehydrogenase Isozymes from Chlamydomonas reinhardtii

Role of Amination and Transamination in Ammonium Incorporation in Chlamydomonas Reinhardtii

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