Maize HSP101 Plays Important Roles in Both Induced and Basal Thermotolerance and Primary Root Growth

Nieto-Sotelo, J.; Martínez, Luz María; Ponce, Gustavo; Cassab, Gladys I.; Alagón, Alejandro; Meeley, Robert B.; Ribaut, Jean-Marcel; Yang, Runying

doi:10.1105/tpc.010487

Cited by 133 publications

(131 citation statements)

References 51 publications

(56 reference statements)

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“…Antisense and co-suppression of Hsp101 expression, and Hsp101 T-DNA insertional mutation in Arabidopsis have all confirmed that Hsp101 has an essential role in thermotolerance [11]. Similar to Arabidopsis Hsp101, insertional knockouts of Hsp101 in maize were also found to be defective in basal and acquired thermotolerance [12]. Together these findings establish a central role for Hsp101 in the development of acquired thermotolerance in plants.…”

Section: Components Of Induced Tolerancesupporting

confidence: 53%

Acquired tolerance to temperature extremes

Sung

Kaplan

Lee

et al. 2003

Trends in Plant Science

504

334

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Section: Components Of Induced Tolerancesupporting

confidence: 53%

Acquired tolerance to temperature extremes

Sung

Kaplan

Lee

et al. 2003

Trends in Plant Science

504

334

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“…Protein Analysis-Total protein extracts from unpollinated ear shoots were prepared as described (20). Cytosolic protein fractions were obtained after trichloroacetic acid precipitation of post-mitochondrial supernatants.…”

Section: Methodsmentioning

confidence: 99%

Mitochondrial Respiratory Deficiencies Signal Up-regulation of Genes for Heat Shock Proteins

Kuzmin

Карпова

Elthon

et al. 2004

Journal of Biological Chemistry

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The consequences of mitochondrial dysfunction are not limited to the development of oxidative stress or initiation of apoptosis but can result in the establishment of stress tolerance. Using maize mitochondrial mutants, we show that permanent mitochondrial deficiencies trigger novel Ca 2؉ -independent signaling pathways, leading to constitutive expression of genes for molecular chaperones, heat shock proteins (HSPs) of different classes. The signaling to activate hsp genes appears to originate from a reduced mitochondrial transmembrane potential. Upon depolarization of mitochondrial membranes in transient assays, gene induction for mitochondrial HSPs occurred more rapidly than that for cytosolic HSPs. We also demonstrate that in the nematode Caenorhabditis elegans transcription of hsp genes can be induced by RNA interference of nuclear respiratory genes. In both organisms, activation of hsp genes in response to mitochondrial impairment is distinct from their responses to heat shock and is not associated with oxidative stress. Thus, mitochondria-to-nucleus signaling to express a hsp gene network is apparently a widespread retrograde mechanism to facilitate cell defense and survival.

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“…(13) and in the eukaryote S. cerevisiae (35,58). HSP101, a member of the Clp/HSP100 family that is present in plants, has also been shown to be implicated in induced thermotolerance in both Arabidopsis thaliana (53) and maize (45). However, until now, only two clpB genes have been described for grampositive bacteria, those of Streptomyces albus G (20) and L. lactis (27), and no obvious phenotype was associated with the FIG.…”

Section: Discussionmentioning

confidence: 99%

clpB, a Novel Member of theListeria monocytogenesCtsR Regulon, Is Involved in Virulence but Not in General Stress Tolerance

et al. 2004

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Clp-HSP100 ATPases are a widespread family of ubiquitous proteins that occur in both prokaryotes and eukaryotes and play important roles in the folding of newly synthesized proteins and refolding of aggregated proteins. They have also been shown to participate in the virulence of several pathogens, including Listeria monocytogenes. Here, we describe a member of the Clp-HSP100 family of L. monocytogenes that harbors all the characteristics of the ClpB subclass, which is absent in the closely related gram-positive model organism, Bacillus subtilis. Transcriptional analysis of clpB revealed a heat shock-inducible A -type promoter. Potential binding sites for the CtsR regulator of stress response were identified in the promoter region. In vivo and in vitro approaches were used to show that expression of clpB is repressed by CtsR, a finding indicating that clpB is a novel member of the L. monocytogenes CtsR regulon. We showed that ClpB is involved in the pathogenicity of L. monocytogenes since the ⌬clpB mutant is significantly affected by virulence in a murine model of infection; we also demonstrate that this effect is apparently not due to a defect in general stress resistance. Indeed, ClpB is not involved in tolerance to heat, salt, detergent, puromycin, or cold stress, even though its synthesis is inducible by heat shock. However, ClpB was shown to play a role in induced thermotolerance, allowing increased resistance of L. monocytogenes to lethal temperatures. This work gives the first example of a clpB gene directly controlled by CtsR and describes the first role for a ClpB protein in induced thermotolerance and virulence in a gram-positive organism.

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Maize HSP101 Plays Important Roles in Both Induced and Basal Thermotolerance and Primary Root Growth

Cited by 133 publications

References 51 publications

Acquired tolerance to temperature extremes

Acquired tolerance to temperature extremes

Mitochondrial Respiratory Deficiencies Signal Up-regulation of Genes for Heat Shock Proteins

clpB, a Novel Member of theListeria monocytogenesCtsR Regulon, Is Involved in Virulence but Not in General Stress Tolerance

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