scholarly journals Characterization of SMOC-2, a modular extracellular calcium-binding protein

2003 ◽  
Vol 373 (3) ◽  
pp. 805-814 ◽  
Author(s):  
Christian VANNAHME ◽  
Silke GÖSLING ◽  
Mats PAULSSON ◽  
Patrik MAURER ◽  
Ursula HARTMANN
Keyword(s):  
Calcium Binding ◽  
Binding Domain ◽  
The Novel ◽  
Northern Blots ◽  
Calcium Dependent ◽  
Reverse Transcription Pcr ◽  
Ef Hand ◽  
Human And Mouse ◽  
Calcium Binding Domain

We have isolated the novel gene SMOC-2, which encodes a secreted modular protein containing an EF-hand calcium-binding domain homologous to that in BM-40. It further consists of two thyroglobulin-like domains, a follistatin-like domain and a novel domain found only in the homologous SMOC-1. Phylogenetic analysis of the calcium-binding domain sequences showed that SMOC-1 and −2 form a separate group within the BM-40 family. The human and mouse SMOC-2 sequences are coded for by genes consisting of 13 exons located on chromosomes 6 and 17, respectively. Analysis of recombinantly expressed protein showed that SMOC-2 is a glycoprotein with a calcium-dependent conformation. Results from Northern blots and reverse transcription PCR revealed a widespread expression in many tissues.

scholarly journals The Calcium-Dependent Interaction between S100B and the Mitochondrial AAA ATPase ATAD3A and the Role of This Complex in the Cytoplasmic Processing of ATAD3A

2010 ◽  
Vol 30 (11) ◽  
pp. 2724-2736 ◽  
Author(s):  
Benoît Gilquin ◽  
Brian R. Cannon ◽  
Arnaud Hubstenberger ◽  
Boualem Moulouel ◽  
Elin Falk ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Nuclear Translocation ◽  
P53 Protein ◽  
Binding Domain ◽  
Binding Motif ◽  
Temperature Sensitive ◽  
Aaa Atpase ◽  
Calcium Dependent ◽  
Ef Hand ◽  
Cell Growth And Differentiation

ABSTRACT S100 proteins comprise a multigene family of EF-hand calcium binding proteins that engage in multiple functions in response to cellular stress. In one case, the S100B protein has been implicated in oligodendrocyte progenitor cell (OPC) regeneration in response to demyelinating insult. In this example, we report that the mitochondrial ATAD3A protein is a major, high-affinity, and calcium-dependent S100B target protein in OPC. In OPC, ATAD3A is required for cell growth and differentiation. Molecular characterization of the S100B binding domain on ATAD3A by nuclear magnetic resonance (NMR) spectroscopy techniques defined a consensus calcium-dependent S100B binding motif. This S100B binding motif is conserved in several other S100B target proteins, including the p53 protein. Cellular studies using a truncated ATAD3A mutant that is deficient for mitochondrial import revealed that S100B prevents cytoplasmic ATAD3A mutant aggregation and restored its mitochondrial localization. With these results in mind, we propose that S100B could assist the newly synthesized ATAD3A protein, which harbors the consensus S100B binding domain for proper folding and subcellular localization. Such a function for S100B might also help to explain the rescue of nuclear translocation and activation of the temperature-sensitive p53val135 mutant by S100B at nonpermissive temperatures.

scholarly journals Characterization of the Calcium Binding Domain of NADPH Oxidase 5 (NOX5)

2009 ◽  
Vol 96 (3) ◽  
pp. 440a
Author(s):  
Chin-Chuan Wei ◽  
Liu Qi Chen ◽  
Tremylla Johnson
Keyword(s):  
Nadph Oxidase ◽  
Calcium Binding ◽  
Binding Domain ◽  
Nadph Oxidase 5 ◽  
Calcium Binding Domain

Mutation/SNP analysis in EF-hand calcium binding domain of mitochondrial Ca2+ uptake 1 gene in bipolar disorder patients

2016 ◽  
Vol 15 (02) ◽  
pp. 163-173 ◽  
Author(s):  
Roghaiyeh Safari ◽  
Reza Salimi ◽  
Zeliha Tunca ◽  
Aysegul Ozerdem ◽  
Deniz Ceylan ◽  
...  
Keyword(s):  
Bipolar Disorder ◽  
Calcium Binding ◽  
Binding Domain ◽  
Snp Analysis ◽  
Ef Hand ◽  
Calcium Binding Domain

scholarly journals Heterologous Expression and Characterization of the Manganese-Oxidizing Protein from Erythrobacter sp. Strain SD21

2014 ◽  
Vol 80 (21) ◽  
pp. 6837-6842 ◽  
Author(s):  
Katherine Nakama ◽  
Michael Medina ◽  
Ahn Lien ◽  
Jordan Ruggieri ◽  
Krystle Collins ◽  
...  
Keyword(s):  
Calcium Binding ◽  
Sequence Similarity ◽  
Cell Extract ◽  
Binding Domain ◽  
Full Length ◽  
Truncated Protein ◽  
Content Type ◽  
Heme Peroxidase ◽  
Calcium Binding Domain

ABSTRACTThe manganese (Mn)-oxidizing protein (MopA) fromErythrobactersp. strain SD21 is part of a unique enzymatic family that is capable of oxidizing soluble Mn(II). This enzyme contains two domains, an animal heme peroxidase domain, which contains the catalytic site, followed by a C-terminal calcium binding domain. Different from the bacterial Mn-oxidizing multicopper oxidase enzymes, little is known about MopA. To gain a better understanding of MopA and its role in Mn(II) oxidation, the 238-kDa full-length protein and a 105-kDa truncated protein containing only the animal heme peroxidase domain were cloned and heterologously expressed inEscherichia coli. Despite having sequence similarity to a peroxidase, hydrogen peroxide did not stimulate activity, nor was activity significantly decreased in the presence of catalase. Both pyrroloquinoline quinone (PQQ) and hemin increased Mn-oxidizing activity, and calcium was required. TheKmfor Mn(II) of the full-length protein in cell extract was similar to that of the natively expressed protein, but theKmvalue for the truncated protein in cell extract was approximately 6-fold higher than that of the full-length protein, suggesting that the calcium binding domain may aid in binding Mn(II). Characterization of the heterologously expressed MopA has provided additional insight into the mechanism of bacterial Mn(II) oxidation, which will aid in understanding the role of MopA and Mn oxidation in bioremediation and biogeochemical cycling.

Fluorescence characterization of VU-9 calmodulin, an engineered calmodulin with one tryptophan in calcium binding domain III

Biochemistry ◽  
1989 ◽  
Vol 28 (14) ◽  
pp. 6086-6092 ◽  
Author(s):  
Marie Claude Kilhoffer ◽  
Daniel M. Roberts ◽  
Abiodun Adibi ◽  
D. Martin Watterson ◽  
Jacques Haiech
Keyword(s):  
Calcium Binding ◽  
Binding Domain ◽  
Domain Iii ◽  
Calcium Binding Domain
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