Purification of recombinant plant and animal GroES homologs: chloroplast and mitochondrial chaperonin 10 (Q74420379)

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10 November 2019

title

Purification of recombinant plant and animal GroES homologs: chloroplast and mitochondrial chaperonin 10 (English)

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10 November 2019

author name string

P V Viitanen

1

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10 November 2019

K Bacot

2

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10 November 2019

R Dickson

3

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10 November 2019

T Webb

4

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10 November 2019

publication date

1 January 1998

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10 November 2019

published in

Methods in Enzymology

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10 November 2019

volume

290

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10 November 2019

page(s)

218-230

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

10 November 2019

cites work

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Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.

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Molecular chaperone functions of heat-shock proteins

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Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

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Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding

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Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins

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GroE facilitates refolding of citrate synthase by suppressing aggregation

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Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

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7 January 2021

GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms

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Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10

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Affinity Purification, Overexpression, and Characterization of Chaperonin 10 Homologues Synthesized with and without N-terminal Acetylation

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Preparation and application of chaperone-deficient Escherichia coli cell-free translation systems

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Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein

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Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits

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

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Spinach chloroplast cpn21 co-chaperonin possesses two functional domains fused together in a toroidal structure and exhibits nucleotide-dependent binding to plastid chaperonin 60.

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7 January 2021

Functional characterization of the higher plant chloroplast chaperonins.

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Molecular chaperones and protein folding in plants

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The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10.

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7 January 2021

Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent

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7 January 2021

Conserved sequence motifs in bacterial and bacteriophage chaperonins

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7 January 2021

Characterization of a functionally important mobile domain of GroES.

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7 January 2021

Unique composition of plastid chaperonin-60: alpha and beta polypeptide-encoding genes are highly divergent

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7 January 2021

Complementary DNA sequence of bovine cpn10 (Hsp10), a chaperone protein from mitochondria

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Isolation of a cDNA clone specifying rat chaperonin 10, a stress-inducible mitochondrial matrix protein synthesised without a cleavable presequence

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7 January 2021

Identification and cloning of human chaperonin 10 homologue

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7 January 2021

The synthesis and purification of 2'-carboxy-D-arabinitol 1-phosphate, a natural inhibitor of ribulose 1,5-bisphosphate carboxylase, investigated by 31P n.m.r

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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The complete primary structure of rat chaperonin 10 reveals a putative beta alpha beta nucleotide-binding domain with homology to p21ras

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7 January 2021

The crystal structure of the GroES co-chaperonin at 2.8 Å resolution

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7 January 2021

10.1016/S0076-6879(98)90021-0

Identifiers

DOI

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10 November 2019

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