scholarly journals The Implication Inferred from the Expression of Small Heat-Shock Protein Genes in Dinoflagellate Resting Cysts Buried in Marine Sediment

Diversity ◽  
2021 ◽  
Vol 13 (10) ◽  
pp. 471
Author(s):  
Yunyan Deng ◽  
Fengting Li ◽  
Zhangxi Hu ◽  
Caixia Yue ◽  
Ying Zhong Tang
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Marine Sediment ◽  
Higher Plants ◽  
Evolutionary Relationship ◽  
Small Heat Shock Protein ◽  
Ambient Conditions ◽  
Green Algal ◽  
Amino Acid Divergence ◽  
Resting Cysts

Dinoflagellates are unicellular eukaryotic microalgae, occupying pivotal niches in aquatic ecosystems with great ecological, biological, and economic significance. Small heat shock proteins (sHsps) are the most omnipresent, but the least conserved, family of molecular chaperones found in all domains of life. Although their common name (small Hsp) implies to exclusively stress their heat shock-responsive function, many sHsps in fact engage in a variety of physiological processes, from cell growth and proliferation to embryogenesis, development, differentiation, apoptosis, and even to human disease prevention. Recent years have greatly expanded our understanding of sHsps in higher plants; however, comprehensive study aiming to delineate the composition and expression pattern of dinoflagellate sHsp gene family has not yet been performed. In this study, we constructed dinoflagellate-specific environmental cDNA library from marine sediment and sequenced using the third-generation sequencing technique. Screening of sHsp genes from the library returned 13 entries with complete coding regions, which were considered to be transcriptionally activated in the natural community of dinoflagellate resting cysts. All the 13 dinoflagellate sHsps consisted of a solely characteristic α-crystallin domain, covering 88–123 amino acid residues with the typical A-X-X-X-N-G-V-L motif, flanked by variable N- and C-terminal extensions. Multiple alignment revealed considerable amino acid divergence (~26.7% average similarity) among them. An unexpected close relationship was revealed between dinoflagellate and green algal sHsps in the phylogenetic tree, seemingly reflecting a close evolutionary relationship of these sHsps themselves. We confirmed that sHsp mRNAs are expressed during dormancy of the resting cyst assemblages of dinoflagellates that were buried in marine sediment, which raised the possibility that the sHsp expression is part of the machinery of maintaining the dormancy or/and the adaptation to ambient conditions of dinoflagellate resting cysts. Our results, although preliminary, gained an important glance on the universal presence of sHsps in dinoflagellates and their active expressions in the assemblage of resting cysts that were buried in the marine sediment. The essentiality of sHsps functioning in resting cysts necessitate more intensive and extensive investigations on all possible functions of Hsps in dinoflagellates, a group of protists with vital ecological and biological importance.

Evolution and functional diversification of the small heat shock protein/α-crystallin family in higher plants

Planta ◽  
2011 ◽  
Vol 235 (6) ◽  
pp. 1299-1313 ◽  
Author(s):  
Hernán Gabriel Bondino ◽  
Estela Marta Valle ◽  
Arjen ten Have
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Higher Plants ◽  
Small Heat Shock Protein ◽  
Functional Diversification

Characterization of expressed meiotic prophase repeat transcript clones of Lilium: meiosis-specific expression, relatedness, and affinities to small heat shock protein genes

Genome ◽  
1990 ◽  
Vol 33 (1) ◽  
pp. 68-79 ◽  
Author(s):  
Robert A. Bouchard
Keyword(s):  
Heat Shock ◽  
Meiotic Prophase ◽  
Higher Plants ◽  
Small Heat Shock Protein ◽  
Heat Shock Gene ◽  
Cdna Clones ◽  
Restriction Maps ◽  
Specific Expression ◽  
Shock Gene

The inserts of plasmid cDNA clones for transcripts showing meiotic prophase specific expression show cross reassociation to varying degrees of intensity with one another. These clones were recovered from a cDNA library made from Lilium microsporocyte poly(A)+ RNA. RNA-dot and Northern-blot analyses indicate that these clones represent transcripts specific to the meiotic prophase interval in microsporocytes. The transcripts appear to constitute the most abundant class of meiosis-specific poly(A)+ RNAs. At least two subgroups can be distinguished by examining cloned transcripts from genes of this expressed meiotic prophase repeat (EMPR) sequence family. Members of each subgroup have similar although not identical restriction maps and show relatively high but varying fidelities of DNA cross reassociation between members. However, consensus restriction maps of the two subgroups are largely dissimilar and, except at low stringencies, cross reassociation is readily detected only at restriction fragments from a particular conserved internal segment. The DNA sequence of a representative EMPR clone has been determined, and the inferred peptide product has been found to show extensive sequence homology to that of a small heat-shock gene of Glycine max, particularly in the conserved region. Alignment of the sequences for the conserved regions of two EMPR subgroup representatives with the soybean sequence suggests that selection has acted to conserve similar blocks of amino acids in this area. These observations suggest that a major portion of the transcripts produced during the apparently unrelated processes of meiosis and heat shock in higher plants are derived from related gene sequences encoding similar products.Key words: meiosis, transcription, specific cDNA, heat-shock mRNA.

scholarly journals The molecular evolution of the small heat-shock proteins in plants.

Genetics ◽  
1995 ◽  
Vol 141 (2) ◽  
pp. 785-795 ◽  
Author(s):  
E R Waters
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Cellular Localization ◽  
Higher Plants ◽  
Small Heat Shock Protein ◽  
Gene Families ◽  
Small Heat Shock Proteins ◽  
Amino Acid Sequences ◽  
Shock Proteins

Abstract The small heat-shock proteins have undergone a tremendous diversification in plants; whereas only a single small heat-shock protein is found in fungi and many animals, over 20 different small heat-shock proteins are found in higher plants. The small heat-shock proteins in plants have diversified in both sequence and cellular localization and are encoded by at least five gene families. In the study, 44 small heat-shock protein DNA and amino acid sequences were examined, using both phylogenetic analysis and analysis of nucleotide substitution patterns to elucidate the evolutionary history of the small heat-shock proteins. The phylogenetic relationships of the small heat-shock proteins, estimated using parsimony and distance methods, reveal the gene duplication, sequence divergence and gene conversion have all played a role in the evolution of the small heat-shock proteins. Analysis of nonsynonymous substitutions and conservative and radical replacement substitutions )in relation to hydrophobicity) indicates that the small heat-shock protein gene families are evolving at different rates. This suggests that the small heat-shock proteins may have diversified in function as well as in sequence and cellular localization.

Mutant small heat shock protein B3 causes motor neuropathy: Utility of a candidate gene approach

Neurology ◽  
2010 ◽  
Vol 74 (6) ◽  
pp. 502-506 ◽  
Author(s):  
S. J. Kolb ◽  
P. J. Snyder ◽  
E. J. Poi ◽  
E. A. Renard ◽  
A. Bartlett ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Candidate Gene ◽  
Small Heat Shock Protein ◽  
Candidate Gene Approach ◽  
Motor Neuropathy

scholarly journals The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation

2021 ◽  
Vol 22 (5) ◽  
pp. 2591
Author(s):  
Pengfei Ma ◽  
Jie Li ◽  
Lei Qi ◽  
Xiuzhu Dong
Keyword(s):  
Heat Shock ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Small Heat Shock Protein ◽  
Phase Cell ◽  
Molecular Weights ◽  
Oxidative Inactivation ◽  
Methionine Residues ◽  
Shock Proteins ◽  
And Function

Small heat shock proteins (sHsps) are widely distributed among various types of organisms and function in preventing the irreversible aggregation of thermal denaturing proteins. Here, we report that Hsp17.6 from Methanolobus psychrophilus exhibited protection of proteins from oxidation inactivation. The overexpression of Hsp17.6 in Escherichia coli markedly increased the stationary phase cell density and survivability in HClO and H2O2. Treatments with 0.2 mM HClO or 10 mM H2O2 reduced malate dehydrogenase (MDH) activity to 57% and 77%, whereas the addition of Hsp17.6 recovered the activity to 70–90% and 86–100%, respectively. A similar effect for superoxide dismutase oxidation was determined for Hsp17.6. Non-reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis assays determined that the Hsp17.6 addition decreased H2O2-caused disulfide-linking protein contents and HClO-induced degradation of MDH; meanwhile, Hsp17.6 protein appeared to be oxidized with increased molecular weights. Mass spectrometry identified oxygen atoms introduced into the larger Hsp17.6 molecules, mainly at the aspartate and methionine residues. Substitution of some aspartate residues reduced Hsp17.6 in alleviating H2O2- and HClO-caused MDH inactivation and in enhancing the E. coli survivability in H2O2 and HClO, suggesting that the archaeal Hsp17.6 oxidation protection might depend on an “oxidant sink” effect, i.e., to consume the oxidants in environments via aspartate oxidation

The small heat shock protein (HSP) 20 is dynamically associated with the actin cross-linking protein actinin

2003 ◽  
Vol 111 (1) ◽  
pp. 152-157 ◽  
Author(s):  
Deron J Tessier ◽  
Padmini Komalavilas ◽  
Alyssa Panitch ◽  
Lokesh Joshi ◽  
Colleen M Brophy
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Cross Linking
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