Deletion of a Chaperonin 60β Gene Leads to Cell Death in the Arabidopsis lesion initiation 1 Mutant

Ishikawa, Atsushi; Tanaka, Hideaki; Nakai, Masaaki; Asahi, Tadashi

doi:10.1093/pcp/pcg031

Cited by 81 publications

(65 citation statements)

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“…In addition to their well-known functions of protein folding and protection, the chaperonin 60 proteins have also shown a range of intercellular signaling activities. In Arabidopsis, LEN1 was identified as encoding a chloroplast Cpn60 beta and the mutation of the LEN1 impairs molecular chaperone in chloroplasts, and which has lead to cell death [32].…”

Section: Hspsmentioning

confidence: 99%

A proteomic approach in analyzing heat‐responsive proteins in rice leaves

et al. 2007

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The present study investigated rice leaf proteome in response to heat stress. Rice seedlings were subjected to a temperature of 427C and samples were collected 12 and 24 h after treatment. Increased relative ion leakage and lipid peroxidation suggested that oxidative stress frequently was generated in rice leaves exposed to high temperature. 2-DE, coupled with MS, was used to investigate and identify heat-responsive proteins in rice leaves. In order to identify the low-abundant proteins in leaves, samples were prefractionated by 15% PEG. The PEG supernatant and the pellet fraction samples were separated by 2-DE, and visualized by silver or CBB staining. Approximately 1000 protein spots were reproducibly detected on each gel, wherein 73 protein spots were differentially expressed at least at one time point. Of these differentially expressed proteins, a total of 34 and 39 protein spots were found in the PEG supernatant and pellet fractions, respectively. Using MALDI-TOF MS, a total of 48 proteins were identified. These proteins were categorized into classes related to heat shock proteins, energy and metabolism, redox homeostasis, and regulatory proteins. The results of the present study show that a group of low molecular small heat shock proteins (sHSPs) were newly induced by heat stress. Among these sHSPs, a low molecular weight mitochondrial (Mt) sHSP was validated further by Western blot analysis. Furthermore, four differentially accumulated proteins that correspond to antioxidant enzymes were analyzed at the mRNA level, which confirmed the differential gene expression levels, and revealed that transcription levels were not completely concomitant with translation. The identification of some novel proteins in the heat stress response provides new insights that can lead to a better understanding of the molecular basis of heat-sensitivity in plants.

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Section: Hspsmentioning

confidence: 99%

A proteomic approach in analyzing heat‐responsive proteins in rice leaves

et al. 2007

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“…2A, len1 plants are much smaller than wild-type plants. 20) To examine whether the LIN2-dependent tetrapyrrole pathway affects growth, I measured the plant sizes of the double mutants described above (Fig. 3).…”

Section: Resultsmentioning

confidence: 99%

“…len1 and lin2 were described previously. 6,20) cs was a gift from Dr. Mochizuki. hy1 and hy2 were gifts from Dr. Kohchi.…”

Section: Methodsmentioning

confidence: 99%

“…len1 and lin2 plants were isolated from enhancer/promoter trap lines, as described previously. 6,20) The genotypes of len1 and lin2 plants were confirmed by PCR amplification of the T-DNA border flanking sequences with the following primers: len1-1,…”

Section: Methodsmentioning

confidence: 99%

“…20) As LEN1 encodes a chloroplast chaperonin 60 (Cpn60), loss of function of chloroplasts is probably the cause of lesion formation, viz., cell death, in len1 plants. 20) It remains to be determined, however, why lesion formation in len1 plants is suppressed under LD. A genetic analysis has been conducted to identify the mechanisms of lesion formation, cell death, in len1 plants under SD.…”

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confidence: 99%

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Tetrapyrrole Metabolism Is Involved in Lesion Formation, Cell Death, in theArabidopsis lesion initiation 1Mutant

Ishikawa

2005

Bioscience, Biotechnology, and Biochemistry

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Plant Abiotic Stress

Jenks

Hasegawa

2005

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of CBF gene expression in response to low temperature 4.2.4.1 DNA regulatory elements controlling CBF expression 4.2.4.2 Proteins with positive roles in CBF expression 4.2.4.3 Proteins with negative roles in CBF expression 4.2.4.4 Other potential CBF regulatory proteins 4.2.4.5 Light and circadian rhythms 4.2.4.6 Role of calcium 4.2.4.7 Role of ABA 4.3 Conservation of the CBF cold-response pathway 4.3.1 Brassica napus 4.3.2 Tomato 4.3.3 Rice 4.4 Concluding remarks 5 Plant responses to high temperature JANE LARKINDALE, MICHAEL MISHKIND and ELIZABETH VIERLING 5.1 Introduction 5.2 Physiological responses to high temperature 5.2.1 High temperature limits to optimal plant performance 5.2.2 Heat sensitivity of photosynthesis 5.2.3 Heat sensitivity of reproduction 5.3 Cellular acquired thermotolerance 5.4 Heat shock proteins/molecular chaperones 5.4.1 Hsp100/ClpB 5.4.2 Hsp90 5.4.3 Hsp70/DnaK 5.4.4 Hsp60/GroE 5.4.5 The sHSP family of proteins 5.5 Other components of the response to heat 5.5.1 Antioxidant production 5.5.2 Other heat-stress regulated genes 5.5.3 Other heat-protective responses 5.5.4 Mutants defective in heat tolerance 5.5.5 Transgenic plants with altered heat tolerance CONTENTS vii 5.6 Signaling pathways involved in response to heat 5.6.1 Heat shock transcription factors 5.6.2 Other signaling pathways 5.6.3 Abscisic acid 5.6.4 Salicylic acid

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Deletion of a Chaperonin 60β Gene Leads to Cell Death in the Arabidopsis lesion initiation 1 Mutant

Cited by 81 publications

References 30 publications

A proteomic approach in analyzing heat‐responsive proteins in rice leaves

A proteomic approach in analyzing heat‐responsive proteins in rice leaves

Tetrapyrrole Metabolism Is Involved in Lesion Formation, Cell Death, in theArabidopsis lesion initiation 1Mutant

Plant Abiotic Stress

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