Complex Formation of Vipp1 Depends on Its α-Helical PspA-like Domain

Aseeva, Elena; Ossenbühl, Friedrich; Eichacker, Lutz A.; Wanner, Gerhard; Soll, Jürgen; Vothknecht, Ute C.

doi:10.1074/jbc.m401750200

Cited by 93 publications

(132 citation statements)

References 21 publications

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“…In vipp1 (a VIPP -Vesicle Inducing Protein in Plastid 1-deleted mutant), thylakoid membrane formation and chloroplast vesicle transport are abolished, indicating that VIPP1 is essential for thylakoid maintenance by a vesicular pathway. Recent data demonstrate that VIPP1 organizes in a high molecular mass complex closely associated with the inner envelope membrane and suggest that the C-terminus of the protein protrudes from the complex into the stroma of chloroplasts possibly for interaction with some other proteins [77]. Accordingly, soluble VIPP1 interacts with a HSP70B/CDJ2 chaperone pair [78].…”

Section: Transfer From the Plastid Envelope To The Thylakoidsmentioning

confidence: 99%

Glycerolipid transfer for the building of membranes in plant cells

Jouhet

Maréchal

Block

2007

Progress in Lipid Research

130

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Section: Transfer From the Plastid Envelope To The Thylakoidsmentioning

confidence: 99%

Glycerolipid transfer for the building of membranes in plant cells

Jouhet

Maréchal

Block

2007

Progress in Lipid Research

130

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“…Although the tertiary structure of IM30 is not yet resolved, it is clear that IM30 monomers interact and assemble into large oligomeric ring complexes with molecular masses exceeding 2 MDa (5,14). However, from a common building block, not a single ring species is formed, rather IM30 forms various ring structures with different rotational symmetries (5, 14 -16).…”

mentioning

confidence: 99%

“…Based on computational analyses, IM30 contains seven ␣-helices, which are interrupted by small random coil domains, and these ␣-helices are predicted to be involved in the formation of coiled-coil structures (5,6,14,15). Although the tertiary structure of IM30 is not yet resolved, it is clear that IM30 monomers interact and assemble into large oligomeric ring complexes with molecular masses exceeding 2 MDa (5, 14).…”

mentioning

confidence: 99%

“…IM30 does not exhibit membrane spanning helices, as is typical for a canonical transmembrane protein (2, 3), and thus, it appears to peripherally bind to the cytoplasmic surface of the inner envelope/cytoplasmic membrane and TMs (5, 13). In fact, IM30 appears to exist in equilibrium between a soluble and a membrane-attached form (5).Based on computational analyses, IM30 contains seven ␣-helices, which are interrupted by small random coil domains, and these ␣-helices are predicted to be involved in the formation of coiled-coil structures (5,6,14,15). Although the tertiary structure of IM30 is not yet resolved, it is clear that IM30 monomers interact and assemble into large oligomeric ring complexes with molecular masses exceeding 2 MDa (5, 14).…”

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confidence: 99%

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Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and Cyanobacteria

Heidrich

Wulf

Hennig

et al. 2016

Journal of Biological Chemistry

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The IM30 (inner membrane-associated protein of 30 kDa), also known as the Vipp1 (vesicle-inducing protein in plastids 1), has a crucial role in thylakoid membrane biogenesis and maintenance. Recent results suggest that the protein binds peripherally to membranes containing negatively charged lipids. However, although IM30 monomers interact and assemble into large oligomeric ring complexes with different numbers of monomers, it is still an open question whether ring formation is crucial for membrane interaction. Here we show that binding of IM30 rings to negatively charged phosphatidylglycerol membrane surfaces results in a higher ordered membrane state, both in the head group and in the inner core region of the lipid bilayer. Furthermore, by using gold nanorods covered with phosphatidylglycerol layers and single particle spectroscopy, we show that not only IM30 rings but also lower oligomeric IM30 structures interact with membranes, although with higher affinity. Thus, ring formation is not crucial for, and even counteracts, membrane interaction of IM30.Engulfment of an ancient cyanobacterium by a primordial cell has resulted in the development of modern day chloroplasts, the organelles where photosynthesis takes place. Consequently, the fine structures of cyanobacterial cells and chloroplasts share many similarities. Notably, chloroplasts and cyanobacteria both contain an extra internal membrane system, the thylakoid membrane (TM) 2 network. Furthermore, both perform oxygenic photosynthesis, and the TMs harbor all protein complexes and pigments involved in the photosynthetic light reaction. However, although assembly and maintenance of TMs is vital for photosynthesis, the details of TM biogenesis and maintenance are still largely unsolved mysteries (1).In 1994 the IM30 (inner membrane-associated protein of 30 kDa) was discovered in chloroplasts of Pisum sativum (2), and a homologous protein appears to be expressed in almost every organism that is able to conduct oxygenic photosynthesis (2-5). Several in vivo studies have shown that the protein plays an essential role in TM formation and maintenance (reviewed in Ref. 6), e.g. the depletion of the protein in Arabidopsis thaliana or the cyanobacterium Synechocystis sp. PCC 6803 has resulted in a decreased amount of TMs (3, 7-9). Under cold stress conditions, depletion of IM30 resulted in the formation of vesicular structures at the chloroplast inner envelope membrane in Arabidopsis, which led to the name Vipp1 (vesicle inducing protein in plastids 1) (3). Nevertheless, although diverse physiological functions were proposed for IM30 in the past two decades, the exact protein function remained elusive for a long time. Only recently, IM30 has been identified to be able to reorganize lipid bilayer structures and to mediate membrane fusion in chloroplasts and cyanobacteria (10). Similar to its bacterial homolog, the PspA (phage shock protein A), which is involved in a bacterial stress response in situations provoking membrane stress (11), IM30 specifically interacts wi...

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“…These results imply that the Avr proteins are secreted from haustoria into the extrahaustorial matrix and recognized by the intracellularly expressed L proteins, either by their translocation into the host cell or by interaction at the plasma membrane. The differential centrifugation procedure developed for Rpg1 can be applied to infected leaf segments and used to determine the proteins that bind with Rpg1 by using Blue native electrophoresis for isolation of membrane complexes (34,35) possibly by combination with cross-linking procedures for enzymatic active complexes (36). This procedure can supplement the yeast two-hybrid approach and is essential to identify both the avirulence protein and the initial components of the signal transduction chain activated by the Rpg1 protein.…”

Section: Discussionmentioning

confidence: 99%

Subcellular localization and functions of the barley stem rust resistance receptor-like serine/threonine-specific protein kinase Rpg1

Nirmala¹,

Brueggeman²,

Maier³

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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The Rpg1 gene confers resistance to many pathotypes of the stem rust fungus Puccinia graminis f. sp. tritici and has protected barley from serious disease losses for over 60 years. Rpg1 encodes a constitutively expressed protein with two tandem kinase domains. Fractionation by differential centrifugation and aqueous twophase separation of the microsome proteins located Rpg1 mainly in the cytosol but also in the plasma membrane and intracellular membranes. Recombinant Rpg1 autophosphorylates in vitro intramolecularly only serine and threonine amino acids with a preference for Mn 2؉ cations and a Km of 0.15 and a Vmax of 0.47 nmol⅐min ؊1 ⅐mg ؊1 protein. The inability of wild-type Rpg1 to transphosphorylate a recombinant Rpg1 inactivated by sitedirected mutation confirmed that Rpg1 autophosphorylation proceeds exclusively via an intramolecular mechanism. Site-directed mutagenesis of the two adjacent lysine residues in the ATP anchor of the two-kinase domains established that the first of the two tandem kinase domains is nonfunctional and that lysine 461 of the second domain is the catalytically active residue. Transgenic barley, expressing Rpg1 mutated in either the kinase 1 or 2 domains, were fully susceptible to P. graminis f. sp. tritici revealing requirement of both kinase domains for resistance. In planta-expressed Rpg1 mutant protein confirmed that mutation in domain 2, but not 1, rendered the protein incapable of autophosphorylation.cultivar ͉ protein kinase 1 domain ͉ protein kinase 2 domain

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Complex Formation of Vipp1 Depends on Its α-Helical PspA-like Domain

Cited by 93 publications

References 21 publications

Glycerolipid transfer for the building of membranes in plant cells

Glycerolipid transfer for the building of membranes in plant cells

Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and Cyanobacteria

Subcellular localization and functions of the barley stem rust resistance receptor-like serine/threonine-specific protein kinase Rpg1

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