Plant Hsp100/ClpB-like proteins: poorly-analyzed cousins of yeast ClpB machine

Singh, Amanjot; Grover, Anil

doi:10.1007/s11103-010-9682-8

Cited by 37 publications

(22 citation statements)

References 105 publications

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“…In this study, matrices corresponding to HSF bindings sites were noted in the promoters of several DEGs in response to CS, HS and OS (Tables 3, 4) suggesting that HSFs are major players in the stress response. It has earlier been noted that HSPs are induced by a variety of stress conditions [21], [40], [59]–[63]. Wang et al [64] has proposed that a cross-talk exists between HSP/chaperone and other stress responsive mechanisms in plants.…”

Section: Discussionmentioning

confidence: 99%

Genome-Wide Transcriptional Profiles during Temperature and Oxidative Stress Reveal Coordinated Expression Patterns and Overlapping Regulons in Rice

Mittal

Madhyastha²,

Grover

2012

PLoS ONE

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Genome wide transcriptional changes by cold stress, heat stress and oxidative stress in rice seedlings were analyzed. Heat stress resulted in predominant changes in transcripts of heat shock protein and heat shock transcription factor genes, as well as genes associated with synthesis of scavengers of reactive oxygen species and genes that control the level of sugars, metabolites and auxins. Cold stress treatment caused differential expression of transcripts of various transcription factors including desiccation response element binding proteins and different kinases. Transcripts of genes that are part of calcium signaling, reactive oxygen scavenging and diverse metabolic reactions were differentially expressed during cold stress. Oxidative stress induced by hydrogen peroxide treatment, resulted in significant up-regulation in transcript levels of genes related to redox homeostasis and down-regulation of transporter proteins. ROS homeostasis appeared to play central role in response to temperature extremes. The key transcription factors that may underlie the concerted transcriptional changes of specific components in various signal transduction networks involved are highlighted. Co-ordinated expression pattern and promoter architectures based analysis (promoter models and overrepresented transcription factor binding sites) suggested potential regulons involved in stress responses. A considerable overlap was noted at the level of transcription as well as in regulatory modules of differentially expressed genes.

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Section: Discussionmentioning

confidence: 99%

Genome-Wide Transcriptional Profiles during Temperature and Oxidative Stress Reveal Coordinated Expression Patterns and Overlapping Regulons in Rice

Mittal

Madhyastha²,

Grover

2012

PLoS ONE

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“…ScHsp104 expression during HS and metal toxicity is independently mediated by the heat shock factor 1 (Hsf1) and Msn2/Msn4 transcriptional activators, respectively. Hsf1 binds to two heat shock elements (HSEs) and Msn2/Msn4 binds to three stress responsive elements (STREs) present in the ScHsp104 promoter (Singh & Grover, 2010). In maize, five HSEs were reported within the proximal 289 bases of the ZmClpB-C promoter region (Nieto-Sotelo et al, 1999).…”

Section: Genetic Regulation Of Clpb-c Gene Expressionmentioning

confidence: 99%

ClpB/Hsp100 proteins and heat stress tolerance in plants

Mishra

Grover

2015

Critical Reviews in Biotechnology

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High-temperature stress can disrupt cellular proteostasis, resulting in the accumulation of insoluble protein aggregates. For survival under stressful conditions, it is important for cells to maintain a pool of native soluble proteins by preventing and/or dissociating these aggregates. Chaperones such as GroEL/GroES (Hsp60/Hsp10) and DnaK/DnaJ/GrpE (Hsp70/Hsp40/nucleotide exchange factor) help cells minimize protein aggregation. Protein disaggregation is accomplished by chaperones belonging to the Caseinolytic Protease (Clp) family of proteins. ClpB/Hsp100 proteins are strikingly ubiquitous and are found in bacteria, yeast and multi-cellular plants. The expression of these proteins is regulated by heat stress (HS) and developmental cues. Bacteria and yeast contain one and two forms of ClpB proteins, respectively. Plants possess multiple forms of these proteins that are localized to different cellular compartments (i.e. cytoplasm/nucleus, chloroplast or mitochondria). Overwhelming evidence suggests that ClpB/Hsp100 proteins play decisive roles in cell adaptation to HS. Mutant bacteria and yeast cells lacking active ClpB/Hsp100 proteins are critically sensitive to high-temperature stress. Likewise, Arabidopsis, maize and rice mutants lacking cytoplasmic ClpB proteins are very sensitive to heat. In this study, we present the structural and functional attributes of plant ClpB forms.

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“…They are localized to different subcellular compartments, such as cytoplasm, nucleus, mitochondria and plasma membrane (Singh & Grover, 2010). Interestingly HSP100 proteins and also their homologues are absent in Archaea (Large et al, 2009), but they are found in Bacteria and Eukaryotes (Barends et al, 2010).…”

Section: Hsp100 Familymentioning

confidence: 99%