Number of the records: 1
Involvement of the Iron Regulatory Protein from Eisenia andrei Earthworms in the Regulation of Cellular Iron Homeostasis
- 1.
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, ORCIDSource 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 https://doi.org/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