High molecular weight pea leaf protein similar to the groE protein of escherichia coli

Pushkin, Alexander; Tsuprun, Vladimir; Solovjeva, N.A.; Shubin, Vladimir; Evstigneeva, Z. G.; Kretovich, W. L.

doi:10.1016/0167-4838(82)90169-8

Cited by 72 publications

(34 citation statements)

References 11 publications

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“…4C) and mixed particles (Fig. 4B) reveal that both types of oligomers exhibit the well known double toroidal, tetradecameric structure that is characteristic of the natural chloroplast and bacterial cpn60 (2,26). At this level of resolution, both sets of reconstituted particles are morphologically indistinguishable.…”

Section: Line 4)mentioning

confidence: 85%

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Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein Folding

Dickson¹,

Weiss²,

Howard³

et al. 2000

Journal of Biological Chemistry

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Unlike the GroEL homologs of eubacteria and mitochondria, oligomer preparations of the higher plant chloroplast chaperonin 60 (cpn60) consist of roughly equal amounts of two divergent subunits, ␣ and ␤. The functional significance of these isoforms, their structural organization into tetradecamers, and their interactions with the unique binary chloroplast chaperonin 10 (cpn10) have not been elucidated. Toward this goal, we have cloned the ␣ and ␤ subunits of the ch-cpn60 of pea (Pisum sativum), expressed them individually in Escherichia coli, and subjected the purified monomers to in vitro reconstitution experiments. In the absence of other factors, neither subunit (alone or in combination) spontaneously assembles into a higher order structure. However, in the presence of MgATP, the ␤ subunits form tetradecamers in a cooperative reaction that is potentiated by cpn10. In contrast, ␣ subunits only assemble in the presence of ␤ subunits. Although ␤ and ␣/␤ 14-mers are indistinguishable by electron microscopy and can both assist protein folding, their specificities for cpn10 are entirely different. Similar to the authentic chloroplast protein, the reconstituted ␣/␤ 14-mers are functionally compatible with bacterial, mitochondrial, and chloroplast cpn10. In contrast, the folding reaction mediated by the reconstituted ␤ 14-mers is only efficient with mitochondrial cpn10. The ability to reconstitute two types of functional oligomer in vitro provides a unique tool, which will allow us to investigate the mechanism of this unusual chaperonin system.

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Section: Line 4)mentioning

confidence: 85%

“…Like other GroEL homologs, the ch-cpn60 consists of two stacked heptameric rings with 7-fold rotational symmetry (26). However, in contrast to bacteria and mitochondria, purified preparations of the native chloroplast protein contain two divergent subunits, ␣ and ␤ (27)(28), that are no more similar to each other than they are to GroEL (29).…”

mentioning

confidence: 99%

Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein Folding

Dickson¹,

Weiss²,

Howard³

et al. 2000

Journal of Biological Chemistry

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“…These were initially assumed to occur in a stoichiometry of a6ß6 (MUSGROVE etal. 1987); however, more recently the subunits were proposed to be identical to a previously identified 14-meric protein (PUSHKIN et al 1982;HEMMINGSEN et al 1988). It has not finally been proven, however, that the binding protein is a hetero-oligomer.…”

Section: Structure and Propertiesmentioning

confidence: 99%

“…The first member of this family, the GroEL protein from E. coli, was purified and characterized several years ago (HENDRIX 1979;HOHN et al 1979). Other members were identified in chloroplasts (BARRACLOUGHand ELLIS 1980;PUSHKIN et al 1982) and mitochondria HALLBERG 1987, 1988). Sequence analysis shows a considerable conservation between the different proteins (about 46%-54% sequence identity; HEMMINGSEN etal.…”

Section: The Groel/hsp60 Familymentioning

confidence: 99%

Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly and Membrane Translocation of Proteins

Langer¹,

Neupert²

1991

Current Topics in Microbiology and Immunology

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“…E. coli cpn60, the GroEL protein, exists as a large cylindrical oligomer composed of 14 identical monomeric subunits possessing seven-fold rotational symmetry [8,9]. The mitochondrial and chloroplast cpn60s (mit cpn60 and chl cpn60, respectively) show similar tetradecameric architecture [10,11] but the plant protein is unique in that it consists of two types of homologous but non-identical monomers (called ~ and fl polypeptides) [12]. Interaction of cpn60s with their substrates (unfolded proteins) is ATP-dependent and is modulated by smaller chaperonin proteins (also called 'co-chaperonins').…”

Section: Introductionmentioning

confidence: 99%

In vitro dissociation and self‐assembly of three chaperonin 60s: the role of ATP

Lissin

1995

FEBS Letters

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A comparative study has investigated the in vitro dissociation and self-assembly of chaperonin 60 14-mers isolated from E. coli (GroEL), yeast mitochondria and pea chloroplasts. In all cases Mg ~+ inhibits, and low temperature stimulates, the urea-induced dissociation. ATP or ADP in the presence of Mg 2÷ enhance the dissociation of the chaperonins. Re-assembly of the 14-mers from their monomers shows different efficiencies between the three proteins. In all cases, however, self-assembly is stimulated by Mg-adenine nucleotides. Surprisingly, effective self-assembly of GroEL is promoted by 20% glycerol in the absence of ATP. The role of Mg-adenine nucleotides in the dissociation and assembly of the chaperonins is discussed.

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High molecular weight pea leaf protein similar to the groE protein of escherichia coli

Cited by 72 publications

References 11 publications

Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein Folding

Reconstitution of Higher Plant Chloroplast Chaperonin 60 Tetradecamers Active in Protein Folding

Heat Shock Proteins hsp60 and hsp70: Their Roles in Folding, Assembly and Membrane Translocation of Proteins

In vitro dissociation and self‐assembly of three chaperonin 60s: the role of ATP

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