scholarly journals Molecular Characterization of hsp20, Encoding a Small Heat Shock Protein of Bifidobacterium breve UCC2003

2007 ◽  
Vol 73 (14) ◽  
pp. 4695-4703 ◽  
Author(s):  
Marco Ventura ◽  
Carlos Canchaya ◽  
Ziding Zhang ◽  
Gerald F. Fitzgerald ◽  
Douwe van Sinderen
Keyword(s):  
Heat Shock ◽  
Stress Proteins ◽  
Osmotic Shock ◽  
Small Heat Shock Protein ◽  
Bifidobacterium Breve ◽  
Class B ◽  
Close Relationship ◽  
Encoding Gene ◽  
Shock Proteins

ABSTRACT Small heat shock proteins (sHSPs) are members of a diverse family of stress proteins that are important in cells to protect proteins under stressful conditions. Genome analysis of Bifidobacterium breve UCC2003 revealed a single sHSP-encoding gene, which was classified as a hsp20 gene by comparative analyses. Genomic surveillance of available genome sequences indicated that hsp20 homologs are not widely distributed in bacteria. In members of the genus Bifidobacterium, this gene appears to be present in only 7 of the 30 currently described species. Moreover, phylogenetic analysis using all available bacterial and eukaryotic sHSP sequences revealed a close relationship between bifidobacterial HSP20 and the class B sHSPs found in members of the division Firmicutes. The results of this comparative analysis and variation in codon usage content suggest that hsp20 was acquired by certain bifidobacteria through horizontal gene transfer. Analysis by slot blot, Northern blot, and primer extension experiments showed that transcription of hsp20 is strongly induced in response to severe heat shock regimens and by osmotic shock.

scholarly journals Characterization of Two Small Heat Shock Protein Genes (Hsp17.4 and Hs20.3) from Sitodiplosis mosellana, and Their Expression Regulation during Diapause

Insects ◽  
2021 ◽  
Vol 12 (2) ◽  
pp. 119
Author(s):  
Jiajia Zhao ◽  
Qitong Huang ◽  
Guojun Zhang ◽  
Keyan Zhu-Salzman ◽  
Weining Cheng
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Cold Stress ◽  
Small Heat Shock Protein ◽  
Short Term ◽  
Sitodiplosis Mosellana ◽  
Severe Heat Stress ◽  
Carboxy Terminal ◽  
Shock Proteins

Sitodiplosis mosellana, a periodic but devastating wheat pest that escapes temperature extremes in summer and winter by undergoing obligatory diapause. To determine the roles of small heat shock proteins (sHsps) in diapause of S. mosellana, we characterized two sHsp genes, SmHsp17.4 and SmHsp20.3, from this species. Both SmHsps contained the conserved α-crystallin domain and the carboxy-terminal I/VXI/V motif of the sHsp family. SmHsp17.4 had one intron while SmHsp20.3 had none. Quantitative PCR revealed that SmHsp17.4 expression decreased after diapause initiation, but substantially increased during transition to post-diapause quiescence. In contrast, SmHsp20.3 expression was not affected by entry of diapause, but was clearly up-regulated during summer and winter. Short-term more severe heat-stress (≥35 °C) of over-summering larvae or cold-stress (≤−5 °C) of over-wintering larvae could stimulate higher expression of both genes, and SmHsp17.4 was more responsive to cold stress while SmHsp20.3 was more sensitive to heat stress. Notably, transcription of SmHsp17.4, but not SmHsp20.3, in diapausing larvae was inducible by 20-hydroxyecdysone (20E). Recombinant SmHsp17.4 and SmHsp20.3 proteins also displayed significant chaperone functionality. These findings suggest that both SmHsps play key roles in stress tolerance during diapause; and 20E-regulated SmHsp17.4 was also likely involved in diapause termination.

scholarly journals Characterization of a Small Heat Shock Protein, Mx Hsp16.6, of Myxococcus xanthus

2005 ◽  
Vol 187 (15) ◽  
pp. 5236-5241 ◽  
Author(s):  
Mieko Otani ◽  
Toshiyuki Ueki ◽  
Satoshi Kozuka ◽  
Miki Segawa ◽  
Keiji Sano ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Myxococcus Xanthus ◽  
Small Heat Shock Protein ◽  
Insertion Mutation ◽  
Amino Acid Residues ◽  
Gene Encoding ◽  
2D Gel ◽  
Shock Proteins

ABSTRACT A number of heat shock proteins in Myxococcus xanthus were previously identified by two-dimensional (2D) gel electrophoresis. One of these protein was termed Mx Hsp16.6, and the gene encoding Mx Hsp16.6 was isolated. Mx Hsp16.6 consists of 147 amino acid residues and has an estimated molecular weight of 16,642, in accordance with the apparent molecular mass in the 2D gel. An α-crystallin domain, typically conserved in small heat shock proteins, was found in Mx Hsp16.6. Mx Hsp16.6 was not detected during normal vegetative growth but was immediately induced after heat shock. Expression of the hsp16.6 gene was not induced by other stresses, such as starvation, oxidation, and high osmolarity. Mx Hsp16.6 was mostly localized in particles formed after heat shock and precipitated by low-speed centrifugation. Furthermore, Mx Hsp16.6 was detected in highly electron-dense particles in heat-shocked cells by immunoelectron microscopy, suggesting that it forms large complexes with heat-denatured proteins. An insertion mutation in the hsp16.6 gene resulted in lower viability during heat shock and lower acquired thermotolerance. Therefore, it is likely that Mx Hsp16.6 plays critical roles in the heat shock response in M. xanthus.

scholarly journals Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of ‘quasi-ordered’ states

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Amanda F Clouser ◽  
Hannah ER Baughman ◽  
Benjamin Basanta ◽  
Miklos Guttman ◽  
Abhinav Nath ◽  
...  
Keyword(s):  
Heat Shock ◽  
Hybrid Approach ◽  
Small Heat Shock Protein ◽  
Exchange Mass Spectrometry ◽  
Structure And Dynamics ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry ◽  
Shock Proteins ◽  
Structural Insights

Small heat shock proteins (sHSPs) are nature’s ‘first responders’ to cellular stress, interacting with affected proteins to prevent their aggregation. Little is known about sHSP structure beyond its structured α-crystallin domain (ACD), which is flanked by disordered regions. In the human sHSP HSPB1, the disordered N-terminal region (NTR) represents nearly 50% of the sequence. Here, we present a hybrid approach involving NMR, hydrogen-deuterium exchange mass spectrometry, and modeling to provide the first residue-level characterization of the NTR. The results support a model in which multiple grooves on the ACD interact with specific NTR regions, creating an ensemble of ‘quasi-ordered’ NTR states that can give rise to the known heterogeneity and plasticity of HSPB1. Phosphorylation-dependent interactions inform a mechanism by which HSPB1 is activated under stress conditions. Additionally, we examine the effects of disease-associated NTR mutations on HSPB1 structure and dynamics, leveraging our emerging structural insights.

scholarly journals Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of “quasi-ordered” states

2019 ◽  
Author(s):  
Amanda F. Clouser ◽  
Hannah E.R. Baughman ◽  
Benjamin Basanta ◽  
Miklos Guttman ◽  
Abhinav Nath ◽  
...  
Keyword(s):  
Heat Shock ◽  
Hybrid Approach ◽  
Small Heat Shock Protein ◽  
Exchange Mass Spectrometry ◽  
Structure And Dynamics ◽  
Hydrogen Deuterium ◽  
Deuterium Exchange Mass Spectrometry ◽  
Shock Proteins ◽  
Structural Insights

ABSTRACTSmall heat shock proteins (sHPSs) are nature’s “first responders” to cellular stress, interacting with affected proteins to prevent their aggregation. Little is known about sHSP structure beyond its structured α-crystallin domain (ACD), which is flanked by disordered regions. In the human sHSP HSPB1, the disordered N-terminal region (NTR) represents nearly 50% of the sequence. Here, we present a hybrid approach involving NMR, hydrogen-deuterium exchange mass spectrometry, and modeling to provide the first residue-level characterization of the NTR. The results support a model in which multiple grooves on the ACD interact with specific NTR regions, creating an ensemble of “quasi-ordered” NTR states that can give rise to the known heterogeneity and plasticity of HSPB1. Phosphorylation-dependent interactions inform a mechanism by which HSPB1 is activated under stress conditions. Additionally, we examine the effects of disease-associated NTR mutations on HSPB1 structure and dynamics, leveraging our emerging structural insights.

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

scholarly journals hsp26 of Saccharomyces cerevisiae is related to the superfamily of small heat shock proteins but is without a demonstrable function.

1989 ◽  
Vol 9 (11) ◽  
pp. 5265-5271 ◽  
Author(s):  
R E Susek ◽  
S L Lindquist
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mutational Analysis ◽  
Small Heat Shock Protein ◽  
Major Effect ◽  
Selfish Dna ◽  
Dna Elements ◽  
Cloned Gene ◽  
Shock Proteins

Analysis of the cloned gene confirms that hsp26 of Saccharomyces cerevisiae is a member of the small heat shock protein superfamily. Previous mutational analysis failed to demonstrate any function for the protein. Further experiments presented here demonstrate that hsp26 has no obvious regulatory role and no major effect on thermotolerance. It is possible that the small heat shock protein genes originated as primitive viral or selfish DNA elements.

Localization of metallothionein, heat shock protein (Hsp70), and superoxide dismutase expression in Hemidiaptomus roubaui (Copepoda, Crustacea) exposed to cadmium and heat stress

2007 ◽  
Vol 85 (3) ◽  
pp. 362-371 ◽  
Author(s):  
Martine Liberge ◽  
Roxane-M. Barthélémy
Keyword(s):  
Superoxide Dismutase ◽  
Heat Stress ◽  
Heat Shock ◽  
Metal Binding ◽  
Stress Proteins ◽  
Reproductive Function ◽  
Cadmium Stress ◽  
Specific Distribution ◽  
Freshwater Crustacean ◽  
Shock Proteins

Immunohistochemical methods were applied in the present study to investigate the expression of stress proteins such as metallothioneins (MT), which are metal-binding proteins, and heat shock proteins (Hsp70), as well as an antioxidant enzyme (superoxide dismutase, SOD), in the freshwater crustacean copepod Hemidiaptomus roubaui (Richard, 1888) exposed to cadmium or heat stress. The results show a tissue-specific distribution of MT-like protein after cadmium exposure in the brain and in the nerve cord. Cadmium stress did not provoke inducible Hsp70 or SOD expression. Unlike cadmium, heat stress induced the expression of Hsp70 and SOD in the shell glands, a structure involved in the reproductive function, and more particularly in the formation of the diapause egg envelope. MT expression is not induced in animals exposed to heat stress.

scholarly journals Characterization of progesterone receptor binding to the 90- and 70-kDa heat shock proteins.

1991 ◽  
Vol 266 (31) ◽  
pp. 21165-21173 ◽  
Author(s):  
D.B. Schowalter ◽  
W.P. Sullivan ◽  
N.J. Maihle ◽  
A.D. Dobson ◽  
O.M. Conneely ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Progesterone Receptor ◽  
Receptor Binding ◽  
Shock Proteins

Herpes simplex virus type 2 UL14 gene product has heat shock protein(HSP)-like functions

2002 ◽  
Vol 115 (12) ◽  
pp. 2517-2527
Author(s):  
Yohei Yamauchi ◽  
Kaoru Wada ◽  
Fumi Goshima ◽  
Tohru Daikoku ◽  
Kenzo Ohtsuka ◽  
...  
Keyword(s):  
Heat Shock ◽  
Nuclear Translocation ◽  
Osmotic Shock ◽  
Minor Component ◽  
Firefly Luciferase ◽  
Hsp70 Family ◽  
Arginine Residues ◽  
Simplex Virus ◽  
A Minor ◽  
Shock Proteins

The HSV-2 UL14 gene encodes a 32 kDa protein that is a minor component of the viral tegument. The protein relocates other viral proteins such as VP26 and UL33 protein into the nuclei of transiently coexpressing cells(Yamauchi et al., 2001). We found that the protein shared some characteristics of heat shock proteins(HSPs) or molecular chaperones, such as nuclear translocation upon heat shock,ATP deprivation and osmotic shock. Interestingly, a significant homology over a stretch of 15 amino acids was found between an N-terminal region of HSV UL14 protein and the substrate-binding domain of Hsp70 family proteins. Two arginine residues in this region were important for nuclear translocation of VP26. In addition, overexpression of UL14 protein increased the activity of coexpressed firefly luciferase, which suggested that the protein functioned in the folding of newly synthesized luciferase. We thus conclude that UL14 protein can act as a chaperone-like protein in a singly expressed state.

scholarly journals Characterization of the New Metallo-β-Lactamase VIM-13 and Its Integron-Borne Gene from a Pseudomonas aeruginosa Clinical Isolate in Spain

2008 ◽  
Vol 52 (10) ◽  
pp. 3589-3596 ◽  
Author(s):  
Carlos Juan ◽  
Alejandro Beceiro ◽  
Olivia Gutiérrez ◽  
Sebastián Albertí ◽  
Margalida Garau ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Pcr Amplification ◽  
Class 1 Integron ◽  
Negative Results ◽  
New Variant ◽  
Class B ◽  
Class 1 ◽  
Encoding Gene ◽  
Good Agreement

ABSTRACT During a survey conducted to evaluate the incidence of class B carbapenemase (metallo-β-lactamase [MBL])-producing Pseudomonas aeruginosa strains from hospitals in Majorca, Spain, five clinical isolates showed a positive Etest MBL screening test result. In one of them, strain PA-SL2, the presence of a new bla VIM derivative (bla VIM-13) was detected by PCR amplification with bla VIM-1-specific primers followed by sequencing. The bla VIM-13-producing isolate showed resistance to all β-lactams (except aztreonam), gentamicin, tobramycin, and ciprofloxacin. VIM-13 exhibited 93% and 88% amino acid sequence identities with VIM-1 and VIM-2, respectively. bla VIM-13 was cloned in parallel with bla VIM-1, and the resistance profile conferred was analyzed both in Escherichia coli and in P. aeruginosa backgrounds. Compared to VIM-1, VIM-13 conferred slightly higher levels of resistance to piperacillin and lower levels of resistance to ceftazidime and cefepime. VIM-13 and VIM-1 were purified in parallel as well, and their kinetic parameters were compared. The k cat/K m ratios for the antibiotics mentioned above were in good agreement with the MIC data. Furthermore, EDTA inhibited the activity of VIM-13 approximately 25 times less than it inhibited the activity of VIM-1. VIM-13 was harbored in a class 1 integron, along with a new variant (Ala108Thr) of the aminoglycoside-modifying enzyme encoding gene aacA4, which confers resistance to gentamicin and tobramycin. Finally, the VIM-13 integron was apparently located in the chromosome, since transformation and conjugation experiments consistently yielded negative results and the bla VIM-13 probe hybridized only with the genomic DNA.

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