Developmental Regulation of the Plastid Protein Import Apparatus.

Dahlin, Clas; Cline, Kenneth

doi:10.1105/tpc.3.10.1131

Cited by 98 publications

(50 citation statements)

References 32 publications

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“…Proteases are also part of the import apparatus (Robinson and Ellis, 1984) whose activity is modified according to the developmental stage of plastids (Dahlin and Cline, 1991). Aminopeptidases also play a role in the maturation of proteins.…”

Section: Discussionmentioning

confidence: 99%

“…8A). The method we have used for the purification of etioplasts is well adapted for the purification of chloroplasts (Klein and Mullet, 1986;Dahlin and Cline, 1991). Therefore, we have isolated chloroplasts from 8-d etiolated plantlets that had then been re-exposed to light for up to 24 h. The activity of alanyl aminopeptidase in isolated plastids was found to return to baseline level as the Chl content increased (Fig.…”

Section: Repression Of Ala Aminopeptidase Activity By Light and Glcmentioning

confidence: 99%

“…The method of purification was worked out from a number of published methods using low (<2500g) accelerations (Klein and Mullet, 1986;Baumgartner et al, 1989;Dahlin and Cline, 1991), thus minimizing damage to plastids. When crude etioplasts obtained by differential centrifugation were centrifuged on a continuous 5 to 80% Percoll gradient, plastids segregated, at all stages of etiolation, as a broad single peak at a modal density of 1.102 (data not shown).…”

Section: Purification Of Plastids From Sugar Beet Cotyledonsmentioning

confidence: 99%

“…The biogenetic development of chloroplasts from proplastids or etioplasts requires the accumulation of proteins through nuclear gene expression, subsequent protein import, and plastidial gene expression (Dahlin and Cline, 1991) with a regulation at the transcriptional and posttranscriptional levels (Klein and Mullet, 1986). In parallel, degradation of specific proplastidial, or etioplastic, proteins such as NADPH-Pchlide oxidoreductase and other prolamellar body proteins must take place (Dahlin and Cline, 1991). Furthermore, carotenoid and Chl synthesis depends on the activity of plastidial enzymes.…”

mentioning

confidence: 99%

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Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities)

et al. 1994

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Section: Discussionmentioning

confidence: 99%

Section: Repression Of Ala Aminopeptidase Activity By Light and Glcmentioning

confidence: 99%

Section: Purification Of Plastids From Sugar Beet Cotyledonsmentioning

confidence: 99%

mentioning

confidence: 99%

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Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities)

et al. 1994

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“…Developmental regulation of protein import has been reported for tobacco (Nicotiana tabacum) leaf mitochondria (Dessi and Whelan, 1997) and for proplastids compared with mature chloroplasts in wheat (Triticum aestivum; Dahlin and Cline, 1991). However, nothing is known of the ontogeny of plant organelles during the differentiation of infected nodule cells.…”

Section: Figurementioning

confidence: 99%

Dual Intracellular Localization and Targeting of Aminoimidazole Ribonucleotide Synthetase in Cowpea

Goggin¹,

Lipscombe²,

Fedorova³

et al. 2003

Plant Physiology

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De novo purine biosynthesis is localized to both mitochondria and plastids isolated from Bradyrhizobium sp.-infected cells of cowpea (Vigna unguiculata L. Walp) nodules, but several of the pathway enzymes, including aminoimidazole ribonucleotide synthetase (AIRS [EC 6.3.3.1], encoded by Vupur5), are encoded by single genes. Immunolocalization confirmed the presence of AIRS protein in both organelles. Enzymatically active AIRS was purified separately from nodule mitochondria and plastids. N-terminal sequencing showed that these two isoforms matched the Vupur5 cDNA sequence but were processed at different sites following import; the mitochondrial isoform was five amino acids longer than the plastid isoform. Electrospray tandem mass spectrometry of a trypsin digest of mitochondrial AIRS identified two internal peptides identical with the amino acid sequence deduced from Vupur5 cDNA. Western blots of proteins from mitochondria and plastids isolated from root tips showed a single AIRS protein present at low levels in both organelles. 35 S-AIRS protein translated from a Vupur5 cDNA was imported into isolated pea (Pisum sativum) leaf chloroplasts in vitro by an ATPdependent process but not into import-competent mitochondria from several plant and non-plant sources. Components of the mature protein are likely to be important for import because the N-terminal targeting sequence was unable to target green fluorescent protein to either chloroplasts or mitochondria in Arabidopsis leaves. The data confirm localization of the protein translated from the AIRS gene in cowpea to both plastids and mitochondria and that it is cotargeted to both organelles, but the mechanism underlying import into mitochondria has features that are yet to be identified.In root nodules of legumes of the tribe Phaseoleae, symbiotically fixed N 2 is assimilated by de novo purine biosynthesis, after which the purines are oxidized to allantoin and allantoic acid (Atkins and Smith, 2000). It is in this form that fixed N is exported in xylem from the nodule to the shoot. The 10 enzymes of the purine biosynthetic pathway have been well studied in relation to their role in cancer metabolism, and the genes encoding them cloned from a wide variety of organisms. However, in plants, far less is known about the enzymes of the pathway, although genes encoding a number have now been isolated (Atkins and Smith, 2000).The cDNA sequences of all the plant purine biosynthetic (pur) genes studied have 5Ј extensions relative to the coding regions of the corresponding Escherichia coli genes (Senecoff and Meagher, 1993;Chapman et al., 1994;Schnorr et al., 1994Schnorr et al., , 1996Kim et al., 1995;Senecoff et al., 1996;Smith et al., 1998). These extensions potentially encode N-terminal, organelle-targeting sequences and indicate that in contrast to other eukaryotes (Gooljarsingh et al., 2001), the pathway is likely to be organelle-localized in plants. This was confirmed in a recent study that showed that in cowpea (Vigna unguiculata L. Walp) nodules, both the mitochondria ...

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In Vitro Analysis of Chloroplast Protein Import

Smith¹,

Schnell²,

Fitzpatrick

et al. 2003

CP Cell Biology

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This unit describes protocols for isolating chloroplasts from pea (Pisum sativum) and Arabidopsis thaliana for the study of nuclear‐encoded plastid precursor proteins. Chloroplasts from both preparations are competent for the in vitro import of recombinant preproteins synthesized using in vitro translation systems derived from reticulocyte or wheat germ lysates. These assays can be used to test whether a particular protein is targeted to chloroplasts, for analyzing the suborganellar location of newly imported preproteins, or to study the mechanism of import itself.

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Developmental Regulation of the Plastid Protein Import Apparatus.

Cited by 98 publications

References 32 publications

Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities)

Modifications of Etioplasts in Cotyledons during Prolonged Dark Growth of Sugar Beet Seedlings (Identification of Etiolation-Related Plastidial Aminopeptidase Activities)

Dual Intracellular Localization and Targeting of Aminoimidazole Ribonucleotide Synthetase in Cowpea

In Vitro Analysis of Chloroplast Protein Import

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