Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae (Q77478060)

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scientific article published on 01 November 1998

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English	Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae	scientific article published on 01 November 1998

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5 December 2019

Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae (English)

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5 December 2019

Saccharomyces cerevisiae

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M Oka

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5 December 2019

M Nakai

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T Endo

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5 December 2019

C R Lim

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Y Kimata

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K Kohno

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1 November 1998

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5 December 2019

Journal of Biological Chemistry

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5 December 2019

273

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5 December 2019

29727-29737

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5 December 2019

Molecular chaperones in cellular protein folding

1 reference

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21 January 2018

Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family

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Poly(A) tail length of a heat shock protein RNA is increased by severe heat stress, but intron splicing is unaffected

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SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.

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The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 is suppressed by loss of mitochondrial DNA.

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21 January 2018

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

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21 January 2018

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

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Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo

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T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol

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A cytoplasmic chaperonin that catalyzes beta-actin folding

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Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin

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TCP1 complex is a molecular chaperone in tubulin biogenesis

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

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Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin

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Molecular chaperones and the centrosome. A role for TCP-1 in microtubule nucleation

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The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes

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Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo

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Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta

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A yeast TCP-1-like protein is required for actin function in vivo

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21 January 2018

The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex

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The essential yeast Tcp1 protein affects actin and microtubules

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21 January 2018

Purification and reconstitution of HeLa cell microtubules

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The relationship of the rat brain 68 kDa microtubule-associated protein with synaptosomal plasma membranes and with the Drosophila 70 kDa heat-shock protein

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In vitro assembly of multiprotein complexes containing alpha, beta, and gamma tubulin, heat shock protein HSP70, and elongation factor 1 alpha

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21 January 2018

HSP70-related 65 kDa protein of beet yellows closterovirus is a microtubule-binding protein

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21 January 2018

Binding of heat-shock protein 70 (hsp70) to tubulin.

1 reference

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21 January 2018

hsp70 is localized to the centrosome of dividing HeLa cells

1 reference

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21 January 2018

Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment

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21 January 2018

The ADE2 gene from Saccharomyces cerevisiae: sequence and new vectors

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21 January 2018

Expression of heterologous genes in Saccharomyces cerevisiae from vectors utilizing the glyceraldehyde-3-phosphate dehydrogenase gene promoter

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21 January 2018

Saccharomyces cerevisiae KAR2 (BiP) gene expression is induced by loss of cytosolic HSP70/Ssa1p through a heat shock element-mediated pathway

1 reference

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21 January 2018

Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces

1 reference

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21 January 2018

Role of astral microtubules and actin in spindle orientation and migration in the budding yeast, Saccharomyces cerevisiae

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21 January 2018

Astral microtubules are not required for anaphase B in Saccharomyces cerevisiae

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21 January 2018

Cytoplasmic dynein is required for normal nuclear segregation in yeast

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Disruption of mitotic spindle orientation in a yeast dynein mutant

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The JNM1 gene in the yeast Saccharomyces cerevisiae is required for nuclear migration and spindle orientation during the mitotic cell cycle

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Functions of microtubules in the Saccharomyces cerevisiae cell cycle

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Binding of mitochondrial presequences to yeast cytosolic heat shock protein 70 depends on the amphiphilicity of the presequence

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Protein folding in the cell

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21 January 2018

The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates

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Identification of a protein altered in mutants resistant to microtubule inhibitors as a member of the major heat shock protein (hsp70) family

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Microtubule assembly nucleated by isolated centrosomes

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γ-Tubulin is a highly conserved component of the centrosome

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A highly divergent gamma-tubulin gene is essential for cell growth and proper microtubule organization in Saccharomyces cerevisiae

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gamma-Tubulin-like Tub4p of Saccharomyces cerevisiae is associated with the spindle pole body substructures that organize microtubules and is required for mitotic spindle formation

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Identification of a complex between centrin and heat shock proteins in CSF-arrested Xenopus oocytes and dissociation of the complex following oocyte activation

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Heat shock alters centrosome organization leading to mitotic dysfunction and cell death

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Dynamic instability of microtubule growth

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10.1074/JBC.273.45.29727

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9792686%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

PubMed publication ID

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9792686%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

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