Sulfolipid Is a Potential Candidate for Annexin Binding to the Outer Surface of Chloroplast

Seigneurin-Berny, Daphné; Rolland, Norbert; Dorne, Albert-Jean; Joyard, Jacques

doi:10.1006/bbrc.2000.2805

Cited by 30 publications

(11 citation statements)

References 33 publications

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“…Indeed, a spinach annexin was found to bind tightly to the outer surface of chloroplasts (Seigneurin-Berny et al ., 2000). Approximately 50 plastid proteins have been identified to date as having dual localizations (Carrie et al ., 2009).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of chromoplasts from six crop species reveals insights into chromoplast function and development

Wang

Yang

Fei

et al. 2013

Journal of Experimental Botany

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Chromoplasts are unique plastids that accumulate massive amounts of carotenoids. To gain a general and comparative characterization of chromoplast proteins, this study performed proteomic analysis of chromoplasts from six carotenoid-rich crops: watermelon, tomato, carrot, orange cauliflower, red papaya, and red bell pepper. Stromal and membrane proteins of chromoplasts were separated by 1D gel electrophoresis and analysed using nLC-MS/MS. A total of 953–2262 proteins from chromoplasts of different crop species were identified. Approximately 60% of the identified proteins were predicted to be plastid localized. Functional classification using MapMan bins revealed large numbers of proteins involved in protein metabolism, transport, amino acid metabolism, lipid metabolism, and redox in chromoplasts from all six species. Seventeen core carotenoid metabolic enzymes were identified. Phytoene synthase, phytoene desaturase, ζ-carotene desaturase, 9-cis-epoxycarotenoid dioxygenase, and carotenoid cleavage dioxygenase 1 were found in almost all crops, suggesting relative abundance of them among the carotenoid pathway enzymes. Chromoplasts from different crops contained abundant amounts of ATP synthase and adenine nucleotide translocator, which indicates an important role of ATP production and transport in chromoplast development. Distinctive abundant proteins were observed in chromoplast from different crops, including capsanthin/capsorubin synthase and fibrillins in pepper, superoxide dismutase in watermelon, carrot, and cauliflower, and glutathione-S-transferease in papaya. The comparative analysis of chromoplast proteins among six crop species offers new insights into the general metabolism and function of chromoplasts as well as the uniqueness of chromoplasts in specific crop species. This work provides reference datasets for future experimental study of chromoplast biogenesis, development, and regulation in plants.

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Section: Discussionmentioning

confidence: 99%

Proteomic analysis of chromoplasts from six crop species reveals insights into chromoplast function and development

Wang

Yang

Fei

et al. 2013

Journal of Experimental Botany

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“…Although most plant annexins are found in the cytosol, several have also been shown to be located in various compartments, such as the cell wall (Kwon et al , 2005), the plasma membrane (Santoni et al , 1998), the vacuole (Seals and Randall, 1997), the chloroplast envelope membranes (Seigneurin-Berny et al , 2000), or the endoplasmic reticulum (Huh et al , 2010), or to be extracellular (Laohavisit et al , 2009). Similarly to other plant annexins, by means of immunolocalization, Ntann12 was shown to be mainly present in the nucleus (Figs 4, 5).…”

Section: Discussionmentioning

confidence: 99%

Ntann12 annexin expression is induced by auxin in tobacco roots

Baucher

Lowe

Vandeputte

et al. 2011

Journal of Experimental Botany

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Ntann12, encoding a polypeptide homologous to annexins, was found previously to be induced upon infection of tobacco with the bacterium Rhodococcus fascians. In this study, Ntann12 is shown to bind negatively charged phospholipids in a Ca2+-dependent manner. In plants growing in light conditions, Ntann12 is principally expressed in roots and the corresponding protein was mainly immunolocalized in the nucleus. Ntann12 expression was inhibited following plant transfer to darkness and in plants lacking the aerial part. However, an auxin (indole-3-acetic acid) treatment restored the expression of Ntann12 in the root system in dark conditions. Conversely, polar auxin transport inhibitors such as 1-naphthylphthalamic acid (NPA) or 2,3,5-triiodobenzoic acid (TIBA) inhibited Ntann12 expression in light condition. These results indicate that the expression of Ntann12 in the root is linked to the perception of a signal in the aerial part of the plant that is transmitted to the root via polar auxin transport.

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“…The sequence obtained from the 36 kDa polypeptide had 94% identity with an EST sequence of Arabidopsis thaliana corresponding to a cytosolic annexin [36]. Annexin does not contain any transmembrane a-helix.…”

Section: The Specific Case Of Lipid-interacting Proteinsmentioning

confidence: 96%

“…Annexin does not contain any transmembrane a-helix. However, the association of annexin with envelope membranes appears to be due to its ability to interact with outer envelope membrane lipids in a Ca 2+ -dependent manner [36]. The interaction of annexin and MGDG synthase with lipids might be strong enough to remain during chloroformmethanol extraction of envelope proteins.…”

Section: The Specific Case Of Lipid-interacting Proteinsmentioning

confidence: 99%

Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins

et al. 2000

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As a complementary approach to genome projects, proteomic analyses have been set up to identify new gene products. One of the major challenges in proteomics concerns membrane proteins, especially the minor ones. A procedure based on the differential extraction of membrane proteins in chloroform/methanol mixtures, was tested on the two different chloroplast membrane systems: envolope and thylakoid membranes. Combining the use of classical sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and mass spectrometry analyses, this procedure enabled identification of hydrophobic proteins. The propensity of hydrophobic proteins to partition in chloroform/methanol mixtures was directly correlated with the number of amino acid residues/number of putative transmembrane regions (Res/TM ratio). Regardless of the particular case of some lipid-interacting proteins, chloroform/methanol extractions allowed enrichment of hydrophobic proteins and exclusion of hydrophilic proteins from both membrane systems, thus demonstrating the versatility of the procedure.

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Sulfolipid Is a Potential Candidate for Annexin Binding to the Outer Surface of Chloroplast

Cited by 30 publications

References 33 publications

Proteomic analysis of chromoplasts from six crop species reveals insights into chromoplast function and development

Proteomic analysis of chromoplasts from six crop species reveals insights into chromoplast function and development

Ntann12 annexin expression is induced by auxin in tobacco roots

Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins

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