Protein Breakdown and the Heat-Shock Response

Goff, Stephen A.; Voellmy, Richard; Goldberg, Alfred L.

doi:10.1007/978-1-4899-2049-2_9

Cited by 25 publications

(15 citation statements)

References 170 publications

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“…An in crease in the concentration of o^^, resulting from both a decrease in its degradation rate and an increase in its synthesis rate, is thought to be directly responsible for the increased level of heat shock protein synthesis seen during a heat shock . It has been sug gested (Goff and Goldberg 1985;Straus et al 1987;Goff et al 1988) that unfolded proteins generated during a heat shock stabilize o^^ indirectly by competing for in tracellular proteases, such as protease La, and thus de crease the degradation of a^^. Our results suggest that if, indeed, this mechanism is operative, then unfolded pro teins do not need to be degraded rapidly to compete for proteases.…”

Section: Discussionmentioning

confidence: 56%

Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation.

Parsell

Sauer²

1989

Genes Dev.

181

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To test the idea that unfolded protein might act as an intracellular signal for induction of the heat shock response in Escbericbia coli, we examined the synthesis of several heat shock proteins after expression of an unfolded variant of the amino-terminal domain of X repressor. These experiments show that expression of a single mutant protein, and not its wild-type counterpart, is sufficient to induce a heat shock-like response. In addition, by measuring the abilities of unfolded variants of differing proteolytic susceptibilities to induce heat shock protein synthesis and by monitoring heat shock protein synthesis as a function of the amount of a single unfolded protein, we show that it is the concentration of unfolded protein in the cell, and not its degradation, that is important for inducing the heat shock-like response.

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Section: Discussionmentioning

confidence: 56%

Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation.

Parsell

Sauer²

1989

Genes Dev.

181

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“…On the other hand, cells which carry multiple copies of the lon gene on plasrnids and therefore have increased levels of this protease, hydrolyze both abnormal and certain normal proteins at increased rates (Goff and Goldberg, 1987). Similar increases in protease content occur in vivo during the heatshock response (Goff et al, 1984(Goff et al, , 1988Goff and Goldberg, 1985). Such enhanced rates of proteolysis must be highly deleterious, and such cells rapidly lose viability or acquire insertion elements on the plasmid that inactivate the cloned gene.…”

Section: Intracellular Proteases In E Eolimentioning

confidence: 73%

“…incorporation of amino acid analogs or puromycin, protease inhibitors, etc. ), other heat-shock proteins are also induced, as shown by gel electrophoresis (Goff and Goldberg, 3985;Goff et al, 1988). Thus, the appearance of aberrant cell proteins may be a common signal under many adverse conditions for the induction of cell proteases and other heat-shock proteins.…”

Section: Protease Inhibitormentioning

confidence: 99%

“…The cell's major heat-shock proteins, DnaK and GroE, have both been shown to promote the refolding of various unfolded proteins (Ostermannet al, 1989;Rothman, 1989;Zylicz and Georgopoulos, 1989). Thus, when cells generate large amounts of damaged or denatured proteins, expression of the heat-shock response can both stimulate repair of these denatured protein or cause their selective degradation (Pelham, 1986;Goff et al, 1988).…”

Section: Protease Inhibitormentioning

confidence: 99%

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The mechanism and functions of ATP‐dependent proteases in bacterial and animal cells

Goldberg

1992

European Journal of Biochemistry

Self Cite

431

186

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“…The involvement of ubiquitin in the response of eukaryotic cells to heat shock and other stresses is well established (reviewed in [21,221). Polyubiquitin genes are heat-shock genes which have upstrem heat-shock response elements and [25].…”

mentioning

confidence: 99%

Ubiquitin in Chlamydomonas reinhardii

Wettern

Parag

Pollmann

et al. 1990

European Journal of Biochemistry

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Ubiquitin, a highly conserved 76-amino-acid protein, is involved in the response of many types of eukaryotic cells to stress but little is known about its role in lower plants. In the present study we have investigated the distribution of ubiquitin in the unicellular alga Chlamydomonas reinhardii as well as the effect of heat and light stress on its conjugation to cellular proteins. Immunoelectron microscopy shows that ubiquitin is located in the chloroplast, nucleus, cytoplasm, pyrenoid and on the plasma membrane. The location of ubiquitin within chloroplasts has not been observed previously. In immunoblots of whole cell extracts with an antibody to ubiquitin a prominent conjugate band with an apparent molecular mass of 29 kDa and a broad region of high-molecularmass conjugates (apparent molecular mass > 45 kDa) were observed. Exposure of cells to a 41.5 "C heat shock in both the dark and light caused the disappearance of the 29-kDa conjugate and an increase in the high-molecularmass conjugates. After step down to 25 "C the 29-kDa conjugate reappeared while the levels of high-molecularmass conjugates decreased. In light, the recovery of the 29-kDa band was more rapid than in the dark. Photoinhibition alters the ubiquitin conjugation pattern similarly to heat shock, but to a lesser degree. These observations imply that, in Chlamydomonas, ubiquitin has a role in the chloroplast and in the response to heat and light stress.Ubiquitin is involved in a number of basic cellular functions in eukaryotic cells which include intracellular protein degradation, response to stress, the cell cycle and DNA repair (see [l -31 for reviews). In higher plants many components of the ubiquitin system have been identified, but their functions are not as well understood as those of their counterparts in mammalian cells or yeast [4, 51. Little is known about the ubiquitin system of lower plants. Recently the sequence of a ubiquitin extension protein from the unicellular alga, Chlamydomonas reinhardii, has been described and its ubiquitin moiety found to differ by only one amino acid residue from that of higher plants [6].Part of the ubiquitin in the cell is found as the free molecule and part of it is linked covalently to other proteins [7]. In mammalian cells ubiquitin is found in various cell compartments which include cytoplasm, nucleus, lysosomes and autophagic vacuoles [8]. On the plasma membrane ubiquitin is linked to certain hormone receptors [9, 101 and to a lymphocyte homing factor [ll]. Ubiquitin has also been found to be associated with cytoskeletal elements of mammalian cells such as microtubules [12], actin [13] and cellular inclusions associated with neurological diseases [14, 151. Immunoelectron microscopy of oat coleoptiles exposed to red light has revealed ubiquitin in both the cytoplasm and the nucleus as well as in dense bodies containing the Pfr form of phytochrome [16 -191. Ubiquitin has also been found to be conjugated to plant viral coat protein subunits [20].The involvement of ubiquitin in the response of euka...

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Protein Breakdown and the Heat-Shock Response

Cited by 25 publications

References 170 publications

Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation.

Induction of a heat shock-like response by unfolded protein in Escherichia coli: dependence on protein level not protein degradation.

The mechanism and functions of ATP‐dependent proteases in bacterial and animal cells

Ubiquitin in Chlamydomonas reinhardii

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