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Involvement of the Iron Regulatory Protein from Eisenia andrei Earthworms in the Regulation of Cellular Iron Homeostasis

SYSNO ASEP	0435252
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Involvement of the Iron Regulatory Protein from Eisenia andrei Earthworms in the Regulation of Cellular Iron Homeostasis
Author(s)	Procházková, Petra (MBU-M)_{RID, ORCID} Škanta, František (MBU-M)_RID Roubalová, Radka (MBU-M)_{RID, ORCID} Šilerová, Marcela (MBU-M) Dvořák, Jiří (MBU-M)_{RID, ORCID} Bilej, Martin (MBU-M)_{RID, ORCID}
Source Title	PLoS ONE. - : Public Library of Science - ISSN 1932-6203 Roč. 9, č. 10 (2014)
Number of pages	12 s.
Language	eng - English
Country	US - United States
Keywords	MULTIPLE SEQUENCE ALIGNMENT ; ELEMENT-BINDING PROTEIN ; FERRITIN MESSENGER-RNA
Subject RIV	EE - Microbiology, Virology
R&D Projects	ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	EE2.3.20.0055 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
Institutional support	MBU-M - RVO:61388971
UT WOS	000342670800103
DOI	10.1371/journal.pone.0109900
Annotation	Iron homeostasis in cells is regulated by iron regulatory proteins (IRPs) that exist in different organisms. IRPs are cytosolic proteins that bind to iron-responsive elements (IREs) of the 5'- or 3'-untranslated regions (UTR) of mRNAs that encode many proteins involved in iron metabolism. In this study, we have cloned and described a new regulatory protein belonging to the family of IRPs from the earthworm Eisenia andrei (EaIRP). The earthworm IRE site in 5'-UTR of ferritin mRNA most likely folds into a secondary structure that differs from the conventional IRE structures of ferritin due to the absence of a typically unpaired cytosine that participates in protein binding. Prepared recombinant EaIRP and proteins from mammalian liver extracts are able to bind both mammalian and Eisenia IRE structures of ferritin mRNA, although the affinity of the rEaIRP/Eisenia IRE structure is rather low. This result suggests the possible contribution of a conventional IRE structure. When IRP is supplemented with a Fe-S cluster, it can function as a cytosolic aconitase. Cellular cytosolic and mitochondrial fractions, as well as recombinant EaIRP, exhibit aconitase activity that can be abolished by the action of oxygen radicals. The highest expression of EaIRP was detected in parts of the digestive tract. We can assume that earthworms may possess an IRE/IRP regulatory network as a potential mechanism for maintaining cellular iron homeostasis, although the aconitase function of EaIRP is most likely more relevant.
Workplace	Institute of Microbiology
Contact	Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
Year of Publishing	2015

Number of the records: 1