Sequence and structural analysis of artemin based on ferritin: A comparative study

Rasti, Behnam; Shahangian, S. Shirin; Sajedi, Reza H.; Taghdir, Majid; Hasannia, Sadegh; Ranjbar, Bijan

doi:10.1016/j.bbapap.2009.05.005

Cited by 19 publications

(27 citation statements)

References 38 publications

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“…The carboxy-terminal extension of artemin fills the oligomer cavity that in ferritin is used to store iron (De Graaf et al 1990;Chen et al 2003Chen et al , 2007. Artemin is missing all but one residue constituting the ferritin di-iron ferroxidase center, another indication it does not sequester metals (De Graaf et al 1990;Harrison and Arosio 1996;Chen et al 2003Chen et al , 2007Theil and Matzapetakis 2006;Rasti et al 2009). …”

Section: Introductionmentioning

confidence: 98%

The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues

Bojikova-Fournier

King

et al. 2011

Cell Stress and Chaperones

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Diapause-destined embryos of the crustacean, Artemia franciscana, accumulate large amounts of an oligomeric, heat-stable, molecular chaperone termed artemin, a cysteine-enriched ferritin homologue. In this study, cysteines 22, 61, 166, and 172 of artemin were substituted with alanines, respectively yielding ArtC22A, ArtC61A, ArtC166A, and ArtC172A. Wild-type and modified artemins were synthesized in transformed bacteria and purified. As measured by heat-induced denaturation of citrate synthase in vitro, each substitution reduced chaperone activity, with ArtC172A the least active. Protein modeling indicated that C172 is close to a region of surface hydrophobicity, also present in ferritin, suggesting that this site contributes to chaperone activity. Only slight differences in oligomer molecular mass were apparent between artemin variants, but ArtC22A and ArtC61A displayed significantly reduced thermostability, perhaps due to the disruption of an inter-subunit disulphide bridge. In contrast, ArtC172A was thermostable, reflecting the location of C172 on the oligomer surface and that it contributes minimally to artemin stabilization. To our knowledge, this is the initial study of structure/function relationships within a ferritin homologue of importance in diapause and the first to indicate that a defined region of hydrophobicity contributes to artemin and ferritin chaperoning.

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Section: Introductionmentioning

confidence: 98%

The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues

Bojikova-Fournier

King

et al. 2011

Cell Stress and Chaperones

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“…Artemin only appears in oviparously developing Artemia embryos, making up a fairly high proportion (10-15%) of Artemia cyst proteins [1][2][3][4]; it is therefore also one of its most important proteins. Artemin was first purified and sequenced by Edman degradation [3] and its cDNA was then sequenced from different species including Artemia franciscana [4], Artemia salina [3] and Artemia urmiana [5]. Artemin is extremely heat-stable, confers stability to transfected mammalian cells against heat and H 2 O 2 and inhibits heat-induced aggregation of citrate synthase in vitro.…”

Section: Introductionmentioning

confidence: 99%

Deletion of extra C-terminal segment and its effect on the function and structure of artemin

Shirzad¹,

Sajedi²,

Shahangian³

et al. 2011

International Journal of Biological Macromolecules

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“…The heat resistance of transformed bacteria synthesizing artemin is enhanced (Rasti et al 2009), and stably transfected mammalian cells containing artemin have increased tolerance to thermal and oxidative stress (Chen et al 2007). That ferritin and artemin are both chaperones suggests that artemin evolved from ferritin to produce an abundant, cyst-specific, molecular chaperone that neither sequesters iron nor disrupts iron metabolism, as would happen if large amounts of intracellular ferritin were synthesized and used as a chaperone.…”

Section: Molecular Chaperones Diapause and Quiescence In Artemiamentioning

confidence: 99%

“…The second abundant cyst protein termed artemin (Slobin 1980) or the 19S complex (De Herdt et al 1979 is similar in amino acid sequence to ferritin, but artemin is enriched in cysteine and possesses an extended carboxylterminal tail not found in ferritin (De Graaf et al 1990;Chen et al 2003;Rasti et al 2009). Artemin has a monomeric molecular mass of 27 kDa and, like ferritin, assembles into oligomers of 24 subunits (Chen et al 2007;Hu et al 2011).…”

Section: Molecular Chaperones Diapause and Quiescence In Artemiamentioning

confidence: 99%

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

MacRae

2016

Cell Stress and Chaperones

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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.

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Sequence and structural analysis of artemin based on ferritin: A comparative study

Cited by 19 publications

References 38 publications

The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues

The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues

Deletion of extra C-terminal segment and its effect on the function and structure of artemin

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

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