Expression of the chloroplast-localized small heat shock protein by oxidative stress in rice

Lee, Byung Hyun; Won, Sung Hye; Lee, Hyo Shin; Miyao, Mitsue; Chung, Woosuk; Kim, In Jung; Jo, Jae Cheol

doi:10.1016/s0378-1119(00)00043-3

Cited by 135 publications

(85 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In addition to heat stress, plant HSPs are also accumulate in response to a large number of other stresses such as heavy metals, oxidative stress, hormones, salt, chilling, and anoxic conditions [7,17,28,29]. In the current study, a total of 18 proteins were identified as HSPs.…”

Section: Hspsmentioning

confidence: 66%

“…The up-regulation or induction of sHSPs has also been noticed in several heat stress related proteomic analyses, which suggest that sHSPs may be used as a biomarker for heat stress [3,11,13]. Earlier, we showed that the overexpression of a rice chloroplast sHSP in Escherichia coli conferred better tolerance not only to heat stress, but it also provided tolerance to oxidative stress [29]. Along with our results, Yeh and coworkers [35] also reported that the overexpression of sHSPs in E. coli showed enhance thermotolerance, as well as changes in the protein aggregation patterns.…”

Section: Hspsmentioning

confidence: 74%

See 1 more Smart Citation

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

et al. 2007

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Hspsmentioning

confidence: 66%

Section: Hspsmentioning

confidence: 74%

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

et al. 2007

Self Cite

View full text Add to dashboard Cite

show abstract

“…Cytosolic sHSPs exist as large oligomers (approximately 200-800 kDa) composed solely or primarily of sHSPs. In Oryza sativa and Lycopersicon esculentum, the sHSPs OsHSP26 and HSP22 are induced by H 2 O 2 (Lee et al 2000). Plant cytosolic HSPs can form complexes containing mostly sHSP, but also HSP70 and RNA.…”

Section: Discussionmentioning

confidence: 99%

Analysis of expressed sequence tags from Musa acuminata ssp. burmannicoides, var. Calcutta 4 (AA) leaves submitted to temperature stresses

et al. 2005

View full text Add to dashboard Cite

In order to discover genes expressed in leaves of Musa acuminata ssp. burmannicoides var. Calcutta 4 (AA), from plants submitted to temperature stress, we produced and characterized two full-length enriched cDNA libraries. Total RNA from plants subjected to temperatures ranging from 5°C to 25°C and from 25°C to 45°C was used to produce a COLD and a HOT cDNA library, respectively. We sequenced 1,440 clones from each library. Following quality analysis and vector trimming, we assembled 2,286 sequences from both libraries into 1,019 putative transcripts, consisting of 217 clusters and 802 singletons, which we denoted Musa acuminata assembled expressed sequence tagged (EST) sequences (MaAES). Of these MaAES, 22.87% showed no matches with existing sequences in public databases. A global analysis of the MaAES data set indicated that 10% of the sequenced cDNAs are present in both cDNA libraries, while 42% and 48% are present only in the COLD or in the HOT libraries, respectively. Annotation of the MaAES data set categorized them into 22 functional classes. Of the 2,286 high-quality sequences, 715 (31.28%) originated from full-length cDNA clones and resulted in a set of 149 genes.

show abstract

“…They are also capable of degrading misfolded proteins (Sun et al 2002). HSPs are known to be inducible by various abiotic stresses, including drought, salinity, high and low temperatures, light, ozone and metal stress (Wang et al 2003;Sabehat et al 1998;Lee et al 2000). The comparison of global expression of genes coding HSP and their transcriptional factors (Hsf) in response to different abiotic stresses was recently investigated.…”

Section: Heat Shock Proteinsmentioning

confidence: 99%

Influence of abiotic stresses on plant proteome and metabolome changes

et al. 2013

View full text Add to dashboard Cite

Plant responses to abiotic stresses are very complex phenomena with individual characteristics for various species. Abiotic stresses (e.g. drought, salinity, flooding, cold, heat, UV radiation, heavy metals, etc.) strongly affect plant growth and development. It is estimated that they are the cause of more than 50 % of crop yield losses. Abiotic stresses are known to activate a multigene response resulting in the changes in various proteins and primary and secondary metabolite accumulation. Therefore, proteomic and metabolomic approaches are becoming very important and powerful tools used in studying plants' reaction to various stimuli. Precise analysis of proteome and metabolome is essential for understanding the fundamentals of stress physiology and biochemistry. In this review, we focus on recent reports concerned to the influence of abiotic stresses on changes in the level of different protein groups and metabolite classes. Basic information about physicochemical methods applied to qualitative and quantitative analyses of biopolymers and natural products is also briefly presented.

show abstract

Expression of the chloroplast-localized small heat shock protein by oxidative stress in rice

Cited by 135 publications

References 27 publications

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

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

Analysis of expressed sequence tags from Musa acuminata ssp. burmannicoides, var. Calcutta 4 (AA) leaves submitted to temperature stresses

Influence of abiotic stresses on plant proteome and metabolome changes

Contact Info

Product

Resources

About