ArticlePlanta2003
A 10-kDa class-CI sHsp protects E. coli from oxidative and high-temperature stress.
Article in Planta, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Exogenous Ascorbic Acid Induced Chilling Tolerance in Tomato Plants Through Modulating Metabolism, Osmolytes, Antioxidants, and Transcriptional Regulation of Catalase and Heat Shock Proteins.Plants (Basel, Switzerland) · 2020Article
- Identification of Genes that Control Silk Yield by RNA Sequencing Analysis of Silkworm (Bombyx mori) Strains of Variable Silk Yield.International journal of molecular sciences · 2018Article
- Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity.Scientific reports · 2013Article
- Article
- Comprehensive sequence and expression profile analysis of Hsp20 gene family in rice.Plant molecular biology · 2009Article
- Dual role for tomato heat shock protein 21: protecting photosystem II from oxidative stress and promoting color changes during fruit maturation.The Plant cell · 2005Article
- Characterization of the genomic structures and selective expression profiles of nine class I small heat shock protein genes clustered on two chromosomes in rice (Oryza sativa L.).Plant molecular biology · 2004Article
- Nodulin 22 from Phaseolus vulgaris protects Escherichia coli cells from oxidative stress.Planta · 2004Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report on a new cDNA clone (Qshsp10.4-CI) of a Quercus suber L. class-CI small heat-shock protein (sHsp) obtained from cork (phellem), a highly oxidatively stressed plant tissue. The deduced gene product lacks the C-terminal extension and the consensus I region of the alpha-crystallin domain, being the most C-terminally truncated sHsp reported to date. In an attempt to prove that a protective function is possible for such a truncated sHsp, we overexpressed in Escherichia coli three recombinant sHsp-CIs, one (rQsHsp10.4-CI) showing the same truncation as Qshsp10.4-CI, a second (rN49) lacking the whole alpha-crystallin domain, and a third (rN153) consisting of a full-length sHsp-CI. The overexpression of rN153 and, remarkably, rQsHsp10.4-CI but not rN49 enhanced cell viability under high temperature and, interestingly, under oxidative stress. These results show that the C-terminal extension and the consensus I region of the alpha-crystallin domain are dispensable, but amino acids 1-41 of the alpha-crystallin domain (including the consensus II region) are essential for the protective activity of sHsp-CIs. On the other hand, two-dimensional immunodetection patterns showed accumulation of ca. 10-kDa sHsp-CI immunorelated polypeptides in cork and other oxidatively stressed tissues but not in control and heat-stressed tissues. We discuss the possible role of highly truncated sHsps in relation to oxidative stress.
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Registered trials
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