A modified Escherichia coli chaperonin (groEL) polypeptide synthesized in tobacco and targeted to the chloroplasts. (Q54652325)

2 June 2018

title

A modified Escherichia coli chaperonin (groEL) polypeptide synthesized in tobacco and targeted to the chloroplasts. (English)

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2 June 2018

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H B Wu

1

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2 June 2018

G L Feist

series ordinal

2

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2 June 2018

S M Hemmingsen

series ordinal

3

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2 June 2018

publication date

1 September 1993

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2 June 2018

number of pages

14

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inferred from page(s)

published in

Plant Molecular Biology

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2 June 2018

volume

22

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2 June 2018

issue

6

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2 June 2018

page(s)

1087-1100

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2 June 2018

https://scigraph.springernature.com/pub.10.1007/bf00028979

exact match

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cites work

The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures

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12 December 2020

Suppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genes

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12 December 2020

Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli

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12 December 2020

Identification of a groES-like chaperonin in mitochondria that facilitates protein folding

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12 December 2020

Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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12 December 2020

The universally conserved GroE (Hsp60) chaperonins

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12 December 2020

Stability and Dissociation of the Large Subunit RuBisCO Binding Protein Complex in Vitro and in Organello

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12 December 2020

Protein folding and chaperonins

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12 December 2020

Targeting a foreign protein to chloroplasts using fusions to the transit peptide of a chlorophyll a/b protein

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12 December 2020

Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants

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12 December 2020

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12 December 2020

Factors affecting the separation of photosynthetically competent chloroplasts in gradients of silica sols

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12 December 2020

Assessment of plant chaperonin-60 gene function in Escherichia coli.

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12 December 2020

Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese

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12 December 2020

Expression of plant chaperonin-60 genes in Escherichia coli

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12 December 2020

GroE facilitates refolding of citrate synthase by suppressing aggregation

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12 December 2020

Functional determinants in transit sequences: import and partial maturation by vascular plant chloroplasts of the ribulose-1,5-bisphosphate carboxylase small subunit of Chlamydomonas

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12 December 2020

The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor

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12 December 2020

Host participation in bacteriophage lambda head assembly

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12 December 2020

Comparison of cauliflower mosaic virus 35S and nopaline synthase promoters in transgenic plants

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BinaryAgrobacteriumvectors for plant transformation

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12 December 2020

Purification and properties of ribulosebisphosphate carboxylase large subunit binding protein

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12 December 2020

Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.

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12 December 2020

Transport of proteins into chloroplasts. The precursor of small subunit of ribulose bisphosphate carboxylase is processed to the mature size in two steps

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12 December 2020

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

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12 December 2020

Protein folding in the cell

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12 December 2020

Large plasmid in Agrobacterium tumefaciens essential for crown gall-inducing ability

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12 December 2020

Electron microscopy of the complexes of ribulose-1,5-bisphosphate carboxylase (Rubisco) and Rubisco subunit-binding protein from pea leaves

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12 December 2020

GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

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12 December 2020

Interaction of GroE with an all-beta-protein

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12 December 2020

Mammalian mitochondrial chaperonin 60 functions as a single toroidal ring

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12 December 2020

Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase

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12 December 2020

A simple and general method for transferring genes into plants

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12 December 2020

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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12 December 2020

Synthesis and assembly of bacterial and higher plant Rubisco subunits in Escherichia coli

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12 December 2020

Identification, characterization, and DNA sequence of a functional "double" groES-like chaperonin from chloroplasts of higher plants

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12 December 2020

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

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12 December 2020

Chaperone function: the assembly of ribulose bisphosphate carboxylase-oxygenase

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12 December 2020

An expression cassette for targeting foreign proteins into chloroplasts

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12 December 2020

Demonstration by genetic suppression of interaction of GroE products with many proteins.

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12 December 2020

Functional inactivation of genes by dominant negative mutations

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12 December 2020

Identifiers

DOI

10.1007/BF00028979

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2 June 2018

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2 June 2018