Characterization of a novel EF-hand homologue, CnidEF, in the sea anemone Anthopleura elegantissima

2007 ◽  
Vol 146 (4) ◽  
pp. 551-559 ◽  
Author(s):  
Laura L. Hauck ◽  
Wendy S. Phillips ◽  
Virginia M. Weis
Keyword(s):  
Sea Anemone ◽  
Ef Hand ◽  
Anthopleura Elegantissima

Characterization of two group III potato CDPKs, StCDPK22 and StCDPK24, that contain three EF-Hand motifs in their CLDs

2021 ◽  
Author(s):  
Marcelo Daniel Sciorra ◽  
Elisa Fantino ◽  
Cecilia Eugenia María Grossi ◽  
Rita María Ulloa
Keyword(s):  
Group Iii ◽  
Ef Hand

scholarly journals Identification of a novel type of processing sites in the precursor for the sea anemone neuropeptide Antho-RFamide (

1992 ◽  
Vol 267 (31) ◽  
pp. 22534-22541
Author(s):  
C Schmutzler ◽  
D Darmer ◽  
D Diekhoff ◽  
C.J. Grimmelikhuijzen
Keyword(s):  
Sea Anemone ◽  
Anthopleura Elegantissima

In silico analysis of selenoprotein N (Gallus gallus): absence of EF-hand motif and the role of CUGS-helix domain in antioxidant protection

Metallomics ◽  
2021 ◽  
Vol 13 (3) ◽  
Author(s):  
Shi-Yong Zhu ◽  
Li-Li Liu ◽  
Yue-Qiang Huang ◽  
Xiao-Wei Li ◽  
Milton Talukder ◽  
...  
Keyword(s):  
In Silico ◽  
Common Ancestor ◽  
In Silico Analysis ◽  
Antioxidant Protection ◽  
Jnk Pathway ◽  
Downstream Target ◽  
Ef Hand ◽  
Silico Analysis

Abstract Selenoprotein N (SEPN1) is critical to the normal muscular physiology. Mutation of SEPN1 can raise congenital muscular disorder in human. It is also central to maturation and structure of skeletal muscle in chicken. However, human SEPN1 contained an EF-hand motif, which was not found in chicken. And the biochemical and molecular characterization of chicken SEPN1 remains unclear. Hence, protein domains, transcription factors, and interactions of Ca2+ in SEPN1 were analyzed in silico to provide the divergence and homology between chicken and human in this work. The results showed that vertebrates’ SEPN1 evolved from a common ancestor. Human and chicken's SEPN1 shared a conserved CUGS-helix domain with function in antioxidant protection. SEPN1 might be a downstream target of JNK pathway, and it could respond to multiple stresses. Human's SEPN1 might not combine with Ca2+ with a single EF-hand motif in calcium homeostasis, and chicken SEPN1 did not have the EF-hand motif in the prediction, indicating the EF-hand motif malfunctioned in chicken SEPN1.

Differential protein profiles reflect the different lifestyles of symbiotic and aposymbiotic Anthopleura elegantissima, a sea anemone from temperate waters

1996 ◽  
Vol 199 (4) ◽  
pp. 883-892
Author(s):  
V M Weis ◽  
R P Levine
Keyword(s):  
Steady State ◽  
Regulation Of Gene Expression ◽  
Sea Anemone ◽  
Protein Profiles ◽  
Post Translational Modification ◽  
Two Dimensional Gel Electrophoresis ◽  
Differential Protein ◽  
Algal Symbionts ◽  
Anthopleura Elegantissima ◽  
Endodermal Cells

Mutualistic associations are prevalent in virtually all environments yet relatively little is known about their complex biochemical and molecular integration and regulation. The endosymbiosis between cnidarians such as the sea anemone Anthopleura elegantissima and the photosynthetic dinoflagellate Symbiodinium californium, in which the algal symbionts are housed in vacuoles within animal endodermal cells, is an ideal model for the study of highly integrated associations at the biochemical and molecular levels. This study describes differential protein synthesis between symbiotic A. elegantissima, collected from environments with high levels of light in the intertidal zone and A. elegantissima that naturally lack symbionts (aposymbiotic), collected from nearby deep-shade habitats. Two-dimensional gel electrophoresis profiles of both steady-state and newly synthesized proteins were compared between the two types of animals using scanning densitometry and image analysis. Symbiotic and aposymbiotic animals share a majority of proteins; however, striking differences in several abundant proteins in steady-state profiles occur. Two proteins are unique to symbiotic animals, one at 32 kDa with an isoelectric point (pI) of 7.9 and another at 31 kDa, pI 6.3. Levels of six proteins with an apparent molecular mass of 25 kDa and pI values ranging from 4.8 to 5.5 are greatly enhanced in aposymbiotic animals. Furthermore, profiles of newly synthesized proteins from symbiotic animals contain a unique cluster of proteins ranging from 25 to 30 kDa and pI 6.6 to 6.9. These marked differences in protein profiles must be a reflection either of underlying differences in the regulation of gene expression or in post-translational modification of common proteins. Identifying the symbiosis-specific products present in A. elegantissima and identifying the inter-partner signaling and cues that result in differential expression will provide an insight into the understanding of these highly integrated associations.

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