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In vitro interaction between a chloroplast transit peptide and chloroplast outer envelope lipids is sequence-specific and lipid class-dependent.

Identifieur interne : 003E25 ( Main/Exploration ); précédent : 003E24; suivant : 003E26

In vitro interaction between a chloroplast transit peptide and chloroplast outer envelope lipids is sequence-specific and lipid class-dependent.

Auteurs : P. Pinnaduwage [États-Unis] ; B D Bruce

Source :

RBID : pubmed:8955132

Descripteurs français

English descriptors

Abstract

Interaction of artificial lipid bilayers (liposomes) with the purified transit peptide (SS-tp) of the precursor form of the small subunit for ribulose-2,5-bisphosphate carboxylase/oxygenase (prSSU) has been studied using a vesicle-disruption assay (calcein dye release) and electron microscopy. Employing purified forms of Escherichia coli-expressed prSSU, mature small subunit, glutathione S-transferase-transit peptide fusion protein, and SS-tp in dye release studies demonstrated that lipid interaction is mediated primarily through the transit peptide. Using chemically synthesized peptides (20-mers), the lipid-interacting domain of the transit peptide was partially mapped to the C-terminal 20 amino acids of the transit peptide. Peptides corresponding to other regions of the transit peptide and control peptides promoted significantly less calcein release. Interaction between the transit peptide and the bilayer was very rapid and could not be resolved by stopped-flow fluorometry with a mixing time of <50 ms. Interaction between the peptides and bilayer was also lipid class-dependent. Disruption occurred only when the bilayer contained the galactolipid monogalactosyldiacylglycerol (MGDG). The extent of bilayer disruption directly correlated with the relative concentration of MGDG in the liposome, with maximum calcein release occurring in 20 mol % MGDG liposomes. Lipid bilayers with greater than 20 mol % MGDG could not be achieved as determined by calcein entrapment. Electron microscopy of the liposomes before and after addition of the transit peptide suggested that the transit peptide induced a dramatic reorganization of lipids. These results are discussed in light of a possible mechanism for the early steps in protein transport that may involve polymorphic changes in the envelope membrane organization to include localized non-bilayer HII structures.

DOI: 10.1074/jbc.271.51.32907
PubMed: 8955132


Affiliations:

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Le document en format XML

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<wicri:regionArea>Department of Biochemistry and Cellular & Molecular Biology and The Center for Legume Research, University of Tennessee, Knoxville, Tennessee 37996-0840</wicri:regionArea>
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<term>Amino Acid Sequence</term>
<term>Biological Transport</term>
<term>Carrier Proteins (metabolism)</term>
<term>Cell Compartmentation</term>
<term>Chloroplasts (chemistry)</term>
<term>Chloroplasts (metabolism)</term>
<term>Diglycerides (metabolism)</term>
<term>Galactolipids</term>
<term>Glycolipids (metabolism)</term>
<term>Intracellular Membranes (metabolism)</term>
<term>Intracellular Signaling Peptides and Proteins</term>
<term>Kinetics</term>
<term>Membrane Lipids (metabolism)</term>
<term>Microscopy, Electron</term>
<term>Molecular Sequence Data</term>
<term>Peas</term>
<term>Plant Proteins (metabolism)</term>
<term>Protein Precursors (metabolism)</term>
<term>Protein Sorting Signals (metabolism)</term>
<term>Ribulose-Bisphosphate Carboxylase (chemistry)</term>
<term>Ribulose-Bisphosphate Carboxylase (metabolism)</term>
<term>Structure-Activity Relationship</term>
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<term>Chloroplastes ()</term>
<term>Chloroplastes (métabolisme)</term>
<term>Cinétique</term>
<term>Compartimentation cellulaire</term>
<term>Diglycéride (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Galactolipides</term>
<term>Glycolipides (métabolisme)</term>
<term>Lipides membranaires (métabolisme)</term>
<term>Membranes intracellulaires (métabolisme)</term>
<term>Microscopie électronique</term>
<term>Pois</term>
<term>Protéines de transport (métabolisme)</term>
<term>Protéines et peptides de signalisation intracellulaire</term>
<term>Protéines végétales (métabolisme)</term>
<term>Précurseurs de protéines (métabolisme)</term>
<term>Relation structure-activité</term>
<term>Ribulose bisphosphate carboxylase ()</term>
<term>Ribulose bisphosphate carboxylase (métabolisme)</term>
<term>Signaux de triage des protéines (métabolisme)</term>
<term>Séquence d'acides aminés</term>
<term>Transport biologique</term>
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<term>Ribulose-Bisphosphate Carboxylase</term>
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<term>Carrier Proteins</term>
<term>Diglycerides</term>
<term>Glycolipids</term>
<term>Membrane Lipids</term>
<term>Plant Proteins</term>
<term>Protein Precursors</term>
<term>Protein Sorting Signals</term>
<term>Ribulose-Bisphosphate Carboxylase</term>
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<term>Intracellular Membranes</term>
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<term>Diglycéride</term>
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<term>Lipides membranaires</term>
<term>Membranes intracellulaires</term>
<term>Protéines de transport</term>
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<term>Précurseurs de protéines</term>
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<term>Microscopie électronique</term>
<term>Pois</term>
<term>Protéines et peptides de signalisation intracellulaire</term>
<term>Relation structure-activité</term>
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<div type="abstract" xml:lang="en">Interaction of artificial lipid bilayers (liposomes) with the purified transit peptide (SS-tp) of the precursor form of the small subunit for ribulose-2,5-bisphosphate carboxylase/oxygenase (prSSU) has been studied using a vesicle-disruption assay (calcein dye release) and electron microscopy. Employing purified forms of Escherichia coli-expressed prSSU, mature small subunit, glutathione S-transferase-transit peptide fusion protein, and SS-tp in dye release studies demonstrated that lipid interaction is mediated primarily through the transit peptide. Using chemically synthesized peptides (20-mers), the lipid-interacting domain of the transit peptide was partially mapped to the C-terminal 20 amino acids of the transit peptide. Peptides corresponding to other regions of the transit peptide and control peptides promoted significantly less calcein release. Interaction between the transit peptide and the bilayer was very rapid and could not be resolved by stopped-flow fluorometry with a mixing time of <50 ms. Interaction between the peptides and bilayer was also lipid class-dependent. Disruption occurred only when the bilayer contained the galactolipid monogalactosyldiacylglycerol (MGDG). The extent of bilayer disruption directly correlated with the relative concentration of MGDG in the liposome, with maximum calcein release occurring in 20 mol % MGDG liposomes. Lipid bilayers with greater than 20 mol % MGDG could not be achieved as determined by calcein entrapment. Electron microscopy of the liposomes before and after addition of the transit peptide suggested that the transit peptide induced a dramatic reorganization of lipids. These results are discussed in light of a possible mechanism for the early steps in protein transport that may involve polymorphic changes in the envelope membrane organization to include localized non-bilayer HII structures.</div>
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