Search results for "Vipp1"

showing 4 items of 4 documents

Functional Implications of Multiple IM30 Oligomeric States

2019

The inner membrane-associated protein of 30 kDa (IM30), also known as the vesicle-inducing protein in plastids 1 (Vipp1), is essential for photo-autotrophic growth of cyanobacteria, algae and higher plants. While its exact function still remains largely elusive, it is commonly accepted that IM30 is crucially involved in thylakoid membrane biogenesis, stabilization and/or maintenance. A characteristic feature of IM30 is its intrinsic propensity to form large homo-oligomeric protein complexes. 15 years ago, it has been reported that these supercomplexes have a ring-shaped structure. However, the in vivo significance of these ring structures is not finally resolved yet and the formation of mor…

0106 biological sciences0301 basic medicinePspAmembrane dynamicsmembrane fusionPlant ScienceReviewlcsh:Plant culture01 natural sciencesVipp103 medical and health sciencesMembrane dynamicslcsh:SB1-1110PlastidChemistryLipid bilayer fusionthylakoid membraneCell biology030104 developmental biologyThylakoidheat shock proteinsmembrane stabilizationFunction (biology)BiogenesisIM30010606 plant biology & botanyFrontiers in Plant Science
researchProduct

Proton Leakage Is Sensed by IM30 and Activates IM30-Triggered Membrane Fusion

2020

The inner membrane-associated protein of 30 kDa (IM30) is crucial for the development and maintenance of the thylakoid membrane system in chloroplasts and cyanobacteria. While its exact physiological function still is under debate, it has recently been suggested that IM30 has (at least) a dual function, and the protein is involved in stabilization of the thylakoid membrane as well as in Mg2+-dependent membrane fusion. IM30 binds to negatively charged membrane lipids, preferentially at stressed membrane regions where protons potentially leak out from the thylakoid lumen into the chloroplast stroma or the cyanobacterial cytoplasm, respectively. Here we show in vitro that IM30 membrane binding…

0301 basic medicineChloroplastsMembrane lipidsmembrane fusionMg2+CyanobacteriaThylakoidsCatalysisArticleVipp1Inorganic Chemistrylcsh:Chemistry03 medical and health sciencesMembrane Lipidsquartz crystal microbalanceProtein structureBacterial ProteinsPhysical and Theoretical ChemistryMg<sup>2+</sup>membrane bindingMolecular Biologylcsh:QH301-705.5SpectroscopyMembranes030102 biochemistry & molecular biologyChemistrypHOrganic ChemistrySynechocystisCD spectroscopyLipid bilayer fusionMembrane Proteinsfood and beveragesGeneral Medicinethylakoid membraneComputer Science ApplicationsChloroplastChloroplast stroma030104 developmental biologyMembranelcsh:Biology (General)lcsh:QD1-999CytoplasmThylakoidBiophysicsProtonsIM30Protein BindingInternational Journal of Molecular Sciences
researchProduct

Membrane chaperoning by members of the PspA/IM30 protein family

2017

ABSTRACTPspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning activity of PspA, IM30 and LiaH and propose that larger oligomeric structures bind to stressed membrane regions, followed by oligomer disassembly and membrane stabilization by protein monomers or smaller/different oligomeric scaffolds.

0301 basic medicineDewey Decimal Classification::500 | Naturwissenschaften::570 | Biowissenschaften BiologieProtein familyPspA030106 microbiologyProtein familyBiologyBiochemistryOligomerVipp103 medical and health scienceschemistry.chemical_compoundddc:570membrane stressLiaHlcsh:QH301-705.5BiologyYjfJMembrane stressMembraneMembrane structuremembrane chaperoneMonomerMembrane structureMonomerMembranelcsh:Biology (General)chemistryBiochemistryOligomerMembrane bindingGeneral Agricultural and Biological SciencesIM30PspA/IM30 familyCommunicative &amp; Integrative Biology
researchProduct

Organization into higher-ordered ring structures counteracts membrane binding of IM30, a protein associated with inner membranes in chloroplasts and …

2017

ABSTRACT PspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning activity of PspA, IM30 and LiaH and propose that larger oligomeric structures bind to stressed membrane regions, followed by oligomer disassembly and membrane stabilization by protein monomers or smaller/different oligomeric scaffolds.

YjfJPspAmembrane stressLiaHIM30oligomerVipp1Article Addendummembrane chaperonePspA/IM30 familyCommunicative & Integrative Biology
researchProduct