Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins (Q29620285)

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scientific article (publication date: 8 November 1990)

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English	Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins	scientific article (publication date: 8 November 1990)

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title

Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins (English)

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main subject

protein folding

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mitochondrion

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author name string

Kang PJ

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1

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Ostermann J

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2

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Shilling J

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3

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Neupert W

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4

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Craig EA

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5

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Pfanner N

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6

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language of work or name

English

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publication date

8 November 1990

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published in

Nature

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volume

348

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6297

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page(s)

137-43

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cites work

Biogenesis of mitochondria

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Protein sorting to mitochondria: evolutionary conservations of folding and assembly

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The mitochondrial protein import apparatus

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The heat-shock proteins

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Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae

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A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

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70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria

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70K heat shock related proteins stimulate protein translocation into microsomes

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Heat-shock proteins. Coming in from the cold.

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Purification and properties of groE, a host protein involved in bacteriophage assembly

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Homologous plant and bacterial proteins chaperone oligomeric protein assembly

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Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor

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Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

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Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria

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Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis

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SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein

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SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth

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Molecular cloning of mtp70, a mitochondrial member of the hsp70 family

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A member of the Hsp70 family is localized in mitochondria and resembles Escherichia coli DnaK

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Hsp70 proteins, similar to Escherichia coli DnaK, in chloroplasts and mitochondria of Euglena gracilis

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Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide

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The processing peptidase of yeast mitochondria: the two co-operating components MPP and PEP are structurally related.

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Mitochondrial protein import

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Import pathways of precursor proteins into mitochondria: multiple receptor sites are followed by a common membrane insertion site

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Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites

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Transport of proteins into mitochondria: translocational intermediates spanning contact sites between outer and inner membranes

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7 January 2021

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Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase

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Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors

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Mitochondrial precursor proteins are imported through a hydrophilic membrane environment

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Characterization of translocation contact sites involved in the import of mitochondrial proteins

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Conformational stability of globular proteins

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Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA

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Proteins as molecular chaperones.

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Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells

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Identification of heat shock protein hsp70 homologues in chloroplasts

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KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene

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S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP.

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An Hsp70-like protein in the ER: identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein

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Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.

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Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas

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Assembly of influenza hemagglutinin trimers and its role in intracellular transport

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Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport

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Speculations on the functions of the major heat shock and glucose-regulated proteins

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Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein

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Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro

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Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast

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Assembly of translocation-competent proteoliposomes from detergent-solubilized rough microsomes

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Peptide binding and release by proteins implicated as catalysts of protein assembly

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Heat-shock proteins DnaK and GroEL facilitate export of LacZ hybrid proteins in E. coli.

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Import of proteins into mitochondria: a multi-step process

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Transport and routing of proteins into chloroplasts

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Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae

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Use of protein A-bearing staphylococci for the immunoprecipitation and isolation of antigens from cells

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Identifiers

DOI

10.1038/348137A0

2 references

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PubMed

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1076016

Dimensions Publication ID

1034947732

0 references

OpenCitations bibliographic resource ID

1076016

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1076016

PubMed publication ID

2234077

2 references

stated in

PubMed

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=2234077

retrieved

30 April 2017

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1076016

ResearchGate publication ID

20922149

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