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Author E A Craig

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The diverse roles of J-proteins, the obligate Hsp70 co-chaperone.

E A Craig, P Huang, R Aron, A Andrew,

Hsp70s and J-proteins, which constitute one of the most ubiquitous types of molecular chaperone machineries, function in a wide variety of cellular processes. J-proteins play a central role by stimulating an Hsp70's ATPase activity, thereby stabilizing its interaction with client proteins. However, while all J-proteins serve this core purpose, individual ... Read more >>

Rev. Physiol. Biochem. Pharmacol. (Reviews of physiology, biochemistry and pharmacology)
[2006, 156:1-21]

Cited: 110 times

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A specialized mitochondrial molecular chaperone system: a role in formation of Fe/S centers.

E A Craig, J Marszalek,

Mitochondria contain a specialized system of molecular chaperones that plays a critical role in the biogenesis of Fe/S centers. This Hsp70:J-protein system shows many similarities to the system found in bacteria, but the precise role of neither chaperone system has been defined. However, evidence to date suggests an interaction with ... Read more >>

Cell. Mol. Life Sci. (Cellular and molecular life sciences : CMLS)
[2002, 59(10):1658-1665]

Cited: 55 times

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Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.

C Pfund, P Huang, N Lopez-Hoyo, E A Craig,

Ssbs of Saccharomyces cerevisiae are ribosome-associated molecular chaperones, which can be cross-linked to nascent polypeptide chains. Because Ssbs are members of a divergent subclass of Hsp70s found thus far only in fungi, we asked if the structural requirements for in vivo function were similar to those of "classic" Hsp70s. An ... Read more >>

Mol. Biol. Cell (Molecular biology of the cell)
[2001, 12(12):3773-3782]

Cited: 43 times

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The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme.

T Hon, H C Lee, A Hach, J L Johnson, E A Craig, H Erdjument-Bromage, P Tempst, L Zhang,

In Saccharomyces cerevisiae, heme directly mediates the effects of oxygen on transcription through the heme activator protein Hap1. In the absence of heme, Hap1 is bound by at least four cellular proteins, including Hsp90 and Ydj1, forming a higher-order complex, termed HMC, and its activity is repressed. Here we purified ... Read more >>

Mol. Cell. Biol. (Molecular and cellular biology)
[2001, 21(23):7923-7932]

Cited: 32 times

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An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae.

J L Johnson, E A Craig,

In addition to regulating the ATPase cycle of Hsp70, a second critical role of Hsp40s has been proposed based on in vitro studies: binding to denatured protein substrates, followed by their presentation to Hsp70 for folding. However, the biological importance of this model is challenged by the fact that deletion ... Read more >>

J. Cell Biol. (The Journal of cell biology)
[2001, 152(4):851-856]

Cited: 59 times

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Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae.

C Voisine, Y C Cheng, M Ohlson, B Schilke, K Hoff, H Beinert, J Marszalek, E A Craig,

A minor Hsp70 chaperone of the mitochondrial matrix of Saccharomyces cerevisiae, Ssq1, is involved in the formation or repair of Fe/S clusters and/or mitochondrial iron metabolism. Here, we report evidence that Jac1, a J-type chaperone of the mitochondrial matrix, is the partner of Ssq1 in this process. Reduced activity of ... Read more >>

Proc. Natl. Acad. Sci. U.S.A. (Proceedings of the National Academy of Sciences of the United States of America)
[2001, 98(4):1483-1488]

Cited: 61 times

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Mitochondrial Hsp70 Ssc1: role in protein folding.

Q Liu, J Krzewska, K Liberek, E A Craig,

Ssc1, the major Hsp70 of the mitochondrial matrix, is involved in the translocation of proteins from the cytosol into the matrix and their subsequent folding. To better understand the physiological mechanism of action of this Hsp70, we have undertaken a biochemical analysis of Ssc1 and two mutant proteins, Ssc1--2 and ... Read more >>

J. Biol. Chem. (The Journal of biological chemistry)
[2001, 276(9):6112-6118]

Cited: 59 times

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Role of the mitochondrial Hsp70s, Ssc1 and Ssq1, in the maturation of Yfh1.

C Voisine, B Schilke, M Ohlson, H Beinert, J Marszalek, E A Craig,

The mitochondrial matrix of the yeast Saccharomyces cerevisiae contains two molecular chaperones of the Hsp70 class, Ssc1 and Ssq1. We report that Ssc1 and Ssq1 play sequential roles in the import and maturation of the yeast frataxin homologue (Yfh1). In vitro, radiolabeled Yfh1 was not imported into ssc1-3 mutant mitochondria, ... Read more >>

Mol. Cell. Biol. (Molecular and cellular biology)
[2000, 20(10):3677-3684]

Cited: 44 times

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A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeast.

J L Johnson, E A Craig,

In addition to its roles in translocation of preproteins across membranes, Ydj1 facilitates the maturation of Hsp90 substrates, including mammalian steroid receptors, which activate transcription in yeast in a hormone-dependent manner. To better understand Ydj1's function, we have constructed and analyzed an array of Ydj1 mutants in vivo. Both the ... Read more >>

Mol. Cell. Biol. (Molecular and cellular biology)
[2000, 20(9):3027-3036]

Cited: 32 times

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Intragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains.

J E Davis, C Voisine, E A Craig,

ATP hydrolysis and polypeptide binding, the two key activities of Hsp70 molecular chaperones, are inherent properties of different domains of the protein. The coupling of these two activities is critical because the bound nucleotide determines, in part, the affinity of Hsp70s for protein substrate. In addition, cochaperones of the Hsp40 ... Read more >>

Proc. Natl. Acad. Sci. U.S.A. (Proceedings of the National Academy of Sciences of the United States of America)
[1999, 96(16):9269-9276]

Cited: 42 times

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Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole.

C Satyanarayana, S Schröder-Köhne, E A Craig, P V Schu, M Horst,

Eukaryotic 70 kDa heat shock proteins (Hsp70s) are localized in various cellular compartments and exhibit functions such as protein translocation across membranes, protein folding and assembly. Here we demonstrate that the constitutively expressed members of the yeast cytoplasmic Ssa subfamily, Ssa1/2p, are involved in the transport of the vacuolar hydrolase ... Read more >>

FEBS Lett. (FEBS letters)
[2000, 470(3):232-238]

Cited: 11 times

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The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1.

W Yan, E A Craig,

Hsp40s are ubiquitous, conserved proteins which function with molecular chaperones of the Hsp70 class. Sis1 is an essential Hsp40 of the cytosol of Saccharomyces cerevisiae, thought to be required for initiation of translation. We carried out a genetic analysis to determine the regions of Sis1 required to perform its key ... Read more >>

Mol. Cell. Biol. (Molecular and cellular biology)
[1999, 19(11):7751-7758]

Cited: 76 times

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The protein import motor of mitochondria: unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70.

C Voisine, E A Craig, N Zufall, O von Ahsen, N Pfanner, W Voos,

Mitochondrial heat shock protein 70 (mtHsp70) functions in unfolding, translocation, and folding of imported proteins. Controversial models of mtHsp70 action have been discussed: (1) physical trapping of preproteins is sufficient to explain the various mtHsp70 functions, and (2) unfolding of preproteins requires an active motor function of mtHsp70 ("pulling"). Intragenic ... Read more >>

Cell (Cell)
[1999, 97(5):565-574]

Cited: 132 times

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Suppression of an Hsp70 mutant phenotype in Saccharomyces cerevisiae through loss of function of the chromatin component Sin1p/Spt2p.

B K Baxter, E A Craig,

The Ssa subfamily of Hsp70 molecular chaperones in the budding yeast Saccharomyces cerevisiae has four members, encoded by SSA1, SSA2, SSA3, and SSA4. Deletion of the two constitutively expressed genes, SSA1 and SSA2, results in cells which are slow growing and temperature sensitive. In this study, we demonstrate that an ... Read more >>

J. Bacteriol. (Journal of bacteriology)
[1998, 180(24):6484-6492]

Cited: 9 times

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SSB, encoding a ribosome-associated chaperone, is coordinately regulated with ribosomal protein genes.

N Lopez, J Halladay, W Walter, E A Craig,

Genes encoding ribosomal proteins and other components of the translational apparatus are coregulated to efficiently adjust the protein synthetic capacity of the cell. Ssb, a Saccharomyces cerevisiae Hsp70 cytosolic molecular chaperone, is associated with the ribosome-nascent chain complex. To determine whether this chaperone is coregulated with ribosomal proteins, we studied ... Read more >>

J. Bacteriol. (Journal of bacteriology)
[1999, 181(10):3136-3143]

Cited: 24 times

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A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport.

N Shulga, P James, E A Craig, D S Goldfarb,

Hsp70 has been implicated in nuclear localization signal (NLS)-directed nuclear transport. Saccharomyces cerevisiae contains distinct SSA and SSB gene families of cytosolic Hsp70s. The nucleocytoplasmic localization of Ssa1p and Ssb1p was investigated using green fluorescent protein (GFP) fusions. Whereas GFP-Ssa1p localized both to the nucleus and cytoplasm, GFP-Ssb1p appeared only ... Read more >>

J. Biol. Chem. (The Journal of biological chemistry)
[1999, 274(23):16501-16507]

Cited: 35 times

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Isolation of UBP3, encoding a de-ubiquitinating enzyme, as a multicopy suppressor of a heat-shock mutant strain of S. cerevisiae.

B K Baxter, E A Craig,

Yeast strains lacking functional copies of the two genes SSA1 and SSA2, which encode cytosolic molecular chaperones, are temperature-sensitive. In this report, we describe the isolation of a high-copy suppressor of this temperature sensitivity, UBP3, which encodes a de-ubiquitinating enzyme. We show that ubp3 mutant yeast strains have a mild ... Read more >>

Curr. Genet. (Current genetics)
[1998, 33(6):412-419]

Cited: 15 times

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Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins.

S Kim, B Schilke, E A Craig, A L Horwich,

The nature of chaperone action in the eukaryotic cytosol that assists newly translated cytosolic proteins to reach the native state has remained poorly defined. Actin, tubulin, and Galpha transducin are assisted by the cytosolic chaperonin, CCT, but many other proteins, for example, ornithine transcarbamoylase (OTC), a cytosolic homotrimeric enzyme of ... Read more >>

Proc. Natl. Acad. Sci. U.S.A. (Proceedings of the National Academy of Sciences of the United States of America)
[1998, 95(22):12860-12865]

Cited: 41 times

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Protein folding in vivo: unraveling complex pathways.

J L Johnson, E A Craig,

Cell (Cell)
[1997, 90(2):201-204]

Cited: 99 times

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Molecular chaperones in biology and medicine at Obernai.

J J Bergeron, E A Craig, A L Horwich, T Langer, G Multhoff, D F Smith, L E Hightower,

Cell Stress Chaperones (Cell stress & chaperones)
[1997, 2(4):220-228]

Cited: 0 times

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Mitochondrial preprotein translocase.

N Pfanner, E A Craig, A Hönlinger,

Mitochondria import most of their proteins from the cytosol. Dynamic protein complexes in the mitochondrial outer and inner membranes are responsible for the specific recognition and membrane translocation of preproteins. The preprotein translocase of the outer mitochondrial membrane contains several import receptors and a general import pore. The preprotein translocase ... Read more >>

Annu. Rev. Cell Dev. Biol. (Annual review of cell and developmental biology)
[1997, 13:25-51]

Cited: 95 times

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Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast.

P James, J Halladay, E A Craig,

The two-hybrid system is a powerful technique for detecting protein-protein interactions that utilizes the well-developed molecular genetics of the yeast Saccharomyces cerevisiae. However, the full potential of this technique has not been realized due to limitations imposed by the components available for use in the system. These limitations include unwieldy ... Read more >>

Genetics (Genetics)
[1996, 144(4):1425-1436]

Cited: 1619 times

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Functional specificity among Hsp70 molecular chaperones.

P James, C Pfund, E A Craig,

Molecular chaperones of the 70-kilodalton heat shock protein (Hsp70) class bind to partially unfolded polypeptide substrates and participate in a wide variety of cellular processes. Differences in peptide-binding specificity among Hsp70s have led to the hypothesis that peptide binding determines specific Hsp70 functions. Protein domains were identified that were required ... Read more >>

Science (Science (New York, N.Y.))
[1997, 275(5298):387-389]

Cited: 133 times

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Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae.

B Miao, J E Davis, E A Craig,

Mge1, a GrpE-related protein in the mitochondrial matrix of the budding yeast Saccharomyces cerevisiae, is required for translocation of precursor proteins into mitochondria. The effect of Mge1 on nucleotide release from Ssc1, an Hsp70 of the mitochondrial matrix, was analyzed. The release of both ATP and ADP from Ssc1 was ... Read more >>

J. Mol. Biol. (Journal of molecular biology)
[1997, 265(5):541-552]

Cited: 61 times

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Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins.

S Laloraya, P J Dekker, W Voos, E A Craig, N Pfanner,

Mitochondrial GrpE (Mge1p) is a mitochondrial cochaperone essential for viability of the yeast Saccharomyces cerevisiae. To study the role of Mge1p in the biogenesis of mitochondrial proteins, we isolated a conditional mutant allele of MGE1 which conferred a temperature-sensitive growth phenotype and led to the accumulation of mitochondrial preproteins after ... Read more >>

Mol. Cell. Biol. (Molecular and cellular biology)
[1995, 15(12):7098-7105]

Cited: 40 times

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