Selective resistance to desiccation of nuclear ribonucleic acid synthesis in isolated nuclei of <i>Artemia salina</i> embryos during pre-emergence development

Kondo, Masatoshi

doi:10.1042/bj1580639

Cited by 8 publications

(3 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Artemia cysts endure repeated dehydration/rehydration with little mortality and no adverse effects on transcription, but this treatment kills prenauplii and nauplii (Morris 1971;De Chaffoy and Kondo 1976). Cysts dehydrated to terminate diapause and then rehydrated were examined by electron microscopy, revealing structures common to eukaryotic cells but in a more crowded setting (Morris 1968;Clegg and Trotman 2002).…”

Section: Trehalose and Stress Tolerance In Artemia Cystsmentioning

confidence: 99%

Stress tolerance during diapause and quiescence of the brine shrimp, Artemia

MacRae

2016

Cell Stress and Chaperones

View full text Add to dashboard Cite

Oviparously developing embryos of the brine shrimp, Artemia, arrest at gastrulation and are released from females as cysts before entering diapause, a state of dormancy and stress tolerance. Diapause is terminated by an external signal, and growth resumes if conditions are permissible. However, if circumstances are unfavorable, cysts enter quiescence, a dormant stage that continues as long as adverse conditions persist. Artemia embryos in diapause and quiescence are remarkably resistant to environmental and physiological stressors, withstanding desiccation, cold, heat, oxidation, ultraviolet radiation, and years of anoxia at ambient temperature when fully hydrated. Cysts have adapted to stress in several ways; they are surrounded by a rigid cell wall impermeable to most chemical compounds and which functions as a shield against ultraviolet radiation. Artemia cysts contain large amounts of trehalose, a non-reducing sugar thought to preserve membranes and proteins during desiccation by replacing water molecules and/or contributing to vitrification. Late embryogenesis abundant proteins similar to those in seeds and other anhydrobiotic organisms are found in cysts, and they safeguard cell organelles and proteins during desiccation. Artemia cysts contain abundant amounts of p26, a small heat shock protein, and artemin, a ferritin homologue, both ATPindependent molecular chaperones important in stress tolerance. The evidence provided in this review supports the conclusion that it is the interplay of these protective elements that make Artemia one of the most stress tolerant of all metazoan organisms.

show abstract

Section: Trehalose and Stress Tolerance In Artemia Cystsmentioning

confidence: 99%

Stress tolerance during diapause and quiescence of the brine shrimp, Artemia

MacRae

2016

Cell Stress and Chaperones

View full text Add to dashboard Cite

show abstract

“…The cysts, composed of about 4000 cells and enclosed in a shell impermeable to most molecules, enter diapause, a condition characterized by an extremely low level of metabolic activity (42)(43)(44)(45)(46). They are very resistant to environmental insults including anoxia, temperature extremes, organic solvents, ␥-irradiation, and desiccation (42,43,47). Desiccation is a normal part of this path of development and may be required to break diapause and reinitiate development.…”

mentioning

confidence: 99%

Molecular Characterization of a Small Heat Shock/α-Crystallin Protein in Encysted Artemia Embryos

Liang¹,

Amons²,

Clegg³

et al. 1997

Journal of Biological Chemistry

View full text Add to dashboard Cite

Molecular chaperones protect cells during stress by limiting the denaturation/aggregation of proteins and facilitating their renaturation. In this context, brine shrimp embryos can endure a wide variety of stressful conditions, including temperature extremes, prolonged anoxia, and desiccation, thus encountering shortages of both energy (ATP) and water. How the embryos survive these stresses is the subject of continuing study, a situation true for other organisms facing similar physiological challenges. To approach this question we cloned and sequenced a cDNA for p26, a molecular chaperone specific to oviparous Artemia embryos. p26 is the first representative of the small heat shock/␣-crystallin family from crustaceans to be sequenced, and it possesses the conserved ␣-crystallin domain characteristic of these proteins. The secondary structure of this domain was predicted to consist predominantly of ␤-pleated sheet, and it appeared to lack regions of ␣-helix. Unique properties of the nonconserved amino terminus, which showed weak similarity to nucleolins and fibrillarins, are enrichments in both glycine and arginine. The carboxyl-terminal tail is the longest yet reported for a small heat shock/␣-crystallin protein, and it is hydrophilic, a common attribute of this region. Site-specific differences between amino acids from p26 and other small heat shock/␣-crystallin proteins bring into question the functions proposed for some of these residues. Probing of Southern blots disclosed a multi-gene family for p26, whereas two size classes of p26 mRNA at 0.7 and 1.9 kilobase pairs were seen on Northern blots, the larger probably representing nonprocessed transcripts. Examination of immunofluorescently stained samples with the confocal microscope revealed that a limited portion of intracellular p26 is found in the nuclei of encysted embryos and that it resides within discrete compartments of this organelle. The results in this paper demonstrate clearly that p26 is a novel member of the small heat shock/␣-crystallin family of proteins. These data, in concert with its restriction to embryos undergoing oviparous development, suggest that p26 functions as a molecular chaperone during exposure to stress, perhaps able to limit protein degradation and thus ensure a ready supply of functional proteins when growth is reinitiated.

show abstract

“…The treated embryos were processed according to Slegers and Kondo in buffer C (pH 6.8) containing 10 mM sodium phosphate (equimolar primary and secondary salts), 5 mM MgCl2 and 50 mM NaCl or buffer A (pH 7.6) containing 35 mM Tris/HCl, 20 mM HEPES (N-2-hydroxyethylpiperazine-N'-2-ethane sulfonic acid), 70 mM KCl and 9 mM MgCl2 (with 150 mM sucrose) as indicated in the figure legends. Extraction of RNA.…”

Section: Methodsmentioning

confidence: 99%

Messenger ribonucleoprotein complexes of cryptobiotic embryos of Artemia salina

Slegers¹,

Kondo²

1977

Nucl Acids Res

View full text Add to dashboard Cite

Poly(A)-containing ribonucleoprotein (poly(A)+-RNP) particles in the post-mitochondrial supernatant of cryptobiotic embryos of Artemia salina were characterized by hybridization to [3H]-poly(U). By sucrose isopycnic centrifugation, approximately 2/3 of poly(A)+-RNPs was found to band at 1.27-1.30 (g/cm3) and the rest 1+/3 at 1.20-1.23 (g/cm3) and below 1.20 (g/cm3). The 1.27-1.30 RNPs could be separated into two density classes, 1.27-1.28 and 1.30 (g/cm3) respectively. The latter RNP class was apparently complexed with ribosomal components because they were completely converted to the former RNP class (free RNPs) by 25 mM EDTA treatment. Further, the 1.30 (g/cm3) RNPs were resolved into several RNP species having sedimentation coefficients above 50 S. which were transformed mostly to 20-30 S rnps in the presence of 25 mM EDTA. The free 20-30 S RNPs contained 8-14 S poly(A)+-RNAs, having the highest template activity in a wheat embryo cell-free system, whereas the 1.20-1.23 poly(A)+-RNPs consisted of 10 S and 16 S RNPs, both of which contained 4 S poly(A)-containing sequences without any template activity.

show abstract

Selective resistance to desiccation of nuclear ribonucleic acid synthesis in isolated nuclei of Artemia salina embryos during pre-emergence development

Cited by 8 publications

References 16 publications

Stress tolerance during diapause and quiescence of the brine shrimp, Artemia

Stress tolerance during diapause and quiescence of the brine shrimp, Artemia

Molecular Characterization of a Small Heat Shock/α-Crystallin Protein in Encysted Artemia Embryos

Messenger ribonucleoprotein complexes of cryptobiotic embryos of Artemia salina

Contact Info

Product

Resources

About