NDLI: The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences ☆

Content Provider	PubMed Central
Author	Tomas, Mireia Jordi, Domènech Capdevila, Mercè Bofill, Roger Atrian, Sílvia
Copyright Year	2013
Abstract	Metallothioneins (MTs) constitute a superfamily of ubiquitous metal-binding proteins of low molecular weight and high Cys content. They are involved in metal homeostasis and detoxification, amongst other proposed biological functions. Two MT isoforms (SpMTA and SpMTB) have been reported in the echinoderm Strongylocentrotus purpuratus (sea urchin), both containing 20 Cys residues and presenting extremely similar sequences, although showing distinct tissular and ontogenic expression patterns. Although exhaustive information is available for the Cd(II)-SpMTA complex, this including the full resolution of its 3D structure, no data has been reported concerning either SpMTA Zn(II) and Cu(I) binding properties, or the characterization of SpMTB at protein level. In this work, both the SpMTA and SpMTB isoforms, as well as their separate α and β domains, have been recombinantly synthesized in the presence of Zn(II), Cd(II) or Cu(II), and the corresponding metal complexes have been analyzed using electrospray mass spectrometry, and CD, ICP-AES and UV–vis spectroscopies. The results clearly show a better performance of isoform A when binding Zn(II) and Cd(II), and of isoform B when coordinating Cu(I). Thus, our results confirm the differential metal binding preference of SpMTA and SpMTB, which, together with the reported induction pattern of the respective genes, highlights how also in Echinodermata the MT polymorphism may be linked to the evolution of different physiological roles.
Related Links	http://dx.doi.org/10.1016/j.fob.2013.01.005
Ending Page	100
Page Count	12
Starting Page	89
File Format	PDF
ISSN	22115463
e-ISSN	22115463
Journal	FEBS Open Bio
Volume Number	3
Language	English
Publisher	Elsevier
Publisher Date	2013-01-01
Access Restriction	Open
Rights Holder	Elsevier
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biochemistry, Genetics and Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Structure, spatial, and temporal expression of two sea urchin metallothionein genes, SpMTB1 and SpMTA.

Combinatorial regulation by promoter and intron 1 regions of the metallothionein SpMTA gene in the sea urchin embryo.

Structure of an ectodermally expressed sea urchin metallothionein gene and characterization of its metal-responsive region.

Sea urchin metallothionein sequence: key to an evolutionary diversity.

NAADP binding to its target protein in sea urchin eggs requires phospholipids

Metallothionein genes MTa and MTb expressed under distinct quantitative and tissue-specific regulation in sea urchin embryos.

Stoichiometry and cluster specificity of copper binding to metallothionein: homogeneous metal clusters.

Sea urchin (Anthocidaris crassispina) egg zinc-binding protein. Cellular localization, purification and characterization.

Order of metal binding in metallothionein.

The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences ☆

Similar Documents

Structure, spatial, and temporal expression of two sea urchin metallothionein genes, SpMTB1 and SpMTA.

Combinatorial regulation by promoter and intron 1 regions of the metallothionein SpMTA gene in the sea urchin embryo.

Structure of an ectodermally expressed sea urchin metallothionein gene and characterization of its metal-responsive region.

Sea urchin metallothionein sequence: key to an evolutionary diversity.

NAADP binding to its target protein in sea urchin eggs requires phospholipids

Metallothionein genes MTa and MTb expressed under distinct quantitative and tissue-specific regulation in sea urchin embryos.

Stoichiometry and cluster specificity of copper binding to metallothionein: homogeneous metal clusters.

Sea urchin (Anthocidaris crassispina) egg zinc-binding protein. Cellular localization, purification and characterization.

Order of metal binding in metallothionein.

The sea urchin metallothionein system: Comparative evaluation of the SpMTA and SpMTB metal-binding preferences ☆