Literature DB >> 17746919

Molecular chaperones: the plant connection.

R J Ellis.   

Abstract

Molecular chaperones are a family of unrelated proteins found in all types of cell. They mediate the correct assembly of other polypeptides, but are not components of the mature assembled structures. Chaperones function by binding specifically to interactive protein surfaces that are exposed transiently during many cellular processes and so prevent them from undergoing incorrect interactions that might produce nonfunctional structures. The concept of molecular chaperones originated largely from studies of the chloroplast enzyme rubisco, which fixes carbon dioxide in plant photosynthesis; the function of chaperones forces a rethinking of the principle of protein self-assembly.

Entities:  

Year:  1990        PMID: 17746919     DOI: 10.1126/science.250.4983.954

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  38 in total

1.  Involvement of a chloroplast HSP70 heat shock protein in the integration of a protein (light-harvesting complex protein precursor) into the thylakoid membrane.

Authors:  S Yalovsky; H Paulsen; D Michaeli; P R Chitnis; R Nechushtai
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-15       Impact factor: 11.205

2.  Characterization of mutant forms of the quinoprotein methanol dehydrogenase lacking an essential calcium ion.

Authors:  I W Richardson; C Anthony
Journal:  Biochem J       Date:  1992-11-01       Impact factor: 3.857

Review 3.  Proteolysis in protein import and export: signal peptide processing in eu- and prokaryotes.

Authors:  M Müller
Journal:  Experientia       Date:  1992-02-15

4.  A mutation in the small subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase that reduces the rate of its incorporation into holoenzyme.

Authors:  Z Adam
Journal:  Photosynth Res       Date:  1995-02       Impact factor: 3.573

Review 5.  Protein folding in vivo and renaturation of recombinant proteins from inclusion bodies.

Authors:  A D Guise; S M West; J B Chaudhuri
Journal:  Mol Biotechnol       Date:  1996-08       Impact factor: 2.695

Review 6.  Molecular chaperones and protein folding in plants.

Authors:  R S Boston; P V Viitanen; E Vierling
Journal:  Plant Mol Biol       Date:  1996-10       Impact factor: 4.076

Review 7.  Translational regulation of the heat shock response.

Authors:  J M Sierra; J M Zapata
Journal:  Mol Biol Rep       Date:  1994-05       Impact factor: 2.316

8.  The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo.

Authors:  H Sternlicht; G W Farr; M L Sternlicht; J K Driscoll; K Willison; M B Yaffe
Journal:  Proc Natl Acad Sci U S A       Date:  1993-10-15       Impact factor: 11.205

9.  Structure and expression of a plastid-encoded groEL homologous heat-shock gene in a thermophilic unicellular red alga.

Authors:  U Maid; R Steinmüller; K Zetsche
Journal:  Curr Genet       Date:  1992-05       Impact factor: 3.886

10.  Isolation of a gene encoding a chaperonin-like protein by complementation of yeast amino acid transport mutants with human cDNA.

Authors:  G B Segel; T R Boal; T S Cardillo; F G Murant; M A Lichtman; F Sherman
Journal:  Proc Natl Acad Sci U S A       Date:  1992-07-01       Impact factor: 11.205

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