Molecular Chaperones

Ellis, R. John; Vies, Saskia M. van der

doi:10.1146/annurev.bi.60.070191.001541

Cited by 1,180 publications

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“…The hsp70 family belongs to a group of proteins known as molecular chaperones (Ellis and van der Vies, 1991) that transiently interact with a wide variety of other cellular proteins. One of the functions of chaperones is to stabilize protein conformation and prevent or disrupt protein aggregates under stress conditions (Vierling, 1991).…”

Section: -28 -20-t T T Discussionmentioning

confidence: 99%

The Correlation between Heat-Shock Protein Accumulation and Persistence and Chilling Tolerance in Tomato Fruit

Sabehat¹,

Weiss²,

Lurie³

1996

Plant Physiol.

177

107

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Heating tomato fruit (Lycopersicon esculentum) for 48 h at 38°Cprevented chilling injury from developing after 21 d at 2"C, whereas unheated fruit developed high levels of injury. Although the overall protein pattern as seen by Coomassie blue staining was similar from heated and unheated fruit, some high-and many low-molecularmass proteins were observed in the heated fruit that were absent or present in reduced amounts in unheated fruit. When fruit were injected with [35S]methionine at harvest and then heated, they accumulated high levels of specific radiolabeled proteins that could still be detected after 21 d at 2°C. If the fruit were held at 20°C after heating, the label in the proteins declined rapidly and these fruit were also sensitive to chilling injury. Hsp70 antibody reacted more strongly with proteins from heated and chilled fruit than with proteins from chilled fruit. Hspl8.1 antibody reacted strongly with proteins from heated fruit but not with those from unheated fruit. A 23-kD protein, highly labeled in heated fruit but not in unheated fruit, had its amino terminus sequenced. To our knowledge, this is the first report showing a relationship between the persistence of heat-shock proteins and chilling tolerance in a plant tissue.

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Section: -28 -20-t T T Discussionmentioning

confidence: 99%

The Correlation between Heat-Shock Protein Accumulation and Persistence and Chilling Tolerance in Tomato Fruit

Sabehat¹,

Weiss²,

Lurie³

1996

Plant Physiol.

177

107

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“…If SRP fails to bind, chaperones of the hsp70 class associate with the nascent precursor as it emerges from the ribosome (Beckmann et al, 1990;Nelson et al, 1992). These hsp70 proteins initially function to prevent aggregation of newly synthesized polypeptide chains (Ellis & van der Vies, 1991). Additional chaperones (Atencio & Yaffe, 1992;Caplan et al, 1992), including those that specifically recognize organellar targeting sequences (Ono & Tuboi, 1990;Murakami et al, 1992;Hachiya et al, 1993), may bind during or after translation.…”

Section: Discussionmentioning

confidence: 99%

Import of cytochrome b₂ to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP

et al. 1993

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Cytochrome b2 is synthesized as a precursor in the cytoplasm and imported to the intermembrane space of yeast mitochondria. We show here that the precursor contains a tightly folded heme-binding domain and that translocation of this domain across the outer membrane requires ATP. Surprisingly, it is ATP in the mitochondrial matrix rather than external ATP that drives import of the heme-binding domain. When the folded structure of the heme-binding domain is disrupted by mutation or by urea denaturation, import and correct processing take place in ATP-depleted mitochondria. These results indicate that (1) cytochrome b2 reaches the intermembrane space without completely crossing the inner membrane, and (2) some precursors fold outside the mitochondria but remain translocation-competent, and import of these precursors in vitro does not require ATP-dependent cytosolic chaperone proteins.

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“…It is believed that chaperones function by recognizing structural features of the interactive surfaces that are accessible only during stages in the assembly process, or that appear as a result of stress, such as heat, in an already assembled structure (Ellis & Van der Vies, 1991).…”

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confidence: 99%

“…The introduction of the concept of molecular chaperones does not contradict the self-assembly hypothesis (Anfinsen, 1973) by suggesting that in many cases interactions within and between polypeptides and other molecules play a role in reducing the probability of the formation of incorrect structures (Ellis & Van der Vies, 1991). Proteins are transported into the endoplasmic reticulum, mitochondrion, plastid, and bacterial periplasm, in an unfolded or partially folded form.…”

mentioning

confidence: 99%

Conformational change of chaperone Hsc70 upon binding to a decapeptide: A circular dichroism study

et al. 1993

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The conformation of bovine Hsc70, a 70-kDa heat shock cognate protein, and its conformational change upon binding to decapeptides, was studied by CD spectroscopy and secondary structure prediction (Chou, P.Y. & Fasman, G.D., 1974, Biochemistry 13, 222-245). The CD spectra were analyzed by the LINCOMB method, as well as by the convex constraint analysis (CCA) method (Perczel, A., Park, K., & Fasman, G.D., 1992, Anal. Biochem. 203, 83-93). The result of the CD analysis of Hsc70 (15% a-helix, 24% 0-sheet, 24% @-turn, and 38% remainder) was very similar to the predicted secondary structure for the &sheet (24%) and the &turn (29%). However, there is disagreement between the a-helical content by CD analysis (15%) and the predicted structure (30%). In spite of the fact that the decapeptides contained a considerable amount of 0-sheet (22%), the interaction of the heat shock protein with the peptide resulted in an overall decrease in the content of @-sheet conformation (-15%) of the complex. This may be due to induction of a molten globule state. The result of the CCA analysis indicated that the Hsc70 undergoes a conformational change upon binding the decapeptides.

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Molecular Chaperones

Cited by 1,180 publications

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The Correlation between Heat-Shock Protein Accumulation and Persistence and Chilling Tolerance in Tomato Fruit

The Correlation between Heat-Shock Protein Accumulation and Persistence and Chilling Tolerance in Tomato Fruit

Import of cytochrome b₂ to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP

Conformational change of chaperone Hsc70 upon binding to a decapeptide: A circular dichroism study

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Molecular Chaperones

Cited by 1,180 publications

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The Correlation between Heat-Shock Protein Accumulation and Persistence and Chilling Tolerance in Tomato Fruit

The Correlation between Heat-Shock Protein Accumulation and Persistence and Chilling Tolerance in Tomato Fruit

Import of cytochrome b2 to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP

Conformational change of chaperone Hsc70 upon binding to a decapeptide: A circular dichroism study

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Import of cytochrome b₂ to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP