A unique ferredoxin acts as a player in the low-iron response of photosynthetic organisms
DC Element | Wert | Sprache |
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dc.contributor.author | Schorsch, Michael | |
dc.contributor.author | Kramer, Manuela | |
dc.contributor.author | Goss, Tatjana | |
dc.contributor.author | Eisenhut, Marion | |
dc.contributor.author | Robinson, Nigel | |
dc.contributor.author | Osman, Deenah | |
dc.contributor.author | Wilde, Annegret | |
dc.contributor.author | Sadaf, Shamaila | |
dc.contributor.author | Brueckler, Hendrik | |
dc.contributor.author | Walder, Lorenz | |
dc.contributor.author | Scheibe, Renate | |
dc.contributor.author | Hase, Toshiharu | |
dc.contributor.author | Hanke, Guy T. | |
dc.date.accessioned | 2021-12-23T16:22:56Z | - |
dc.date.available | 2021-12-23T16:22:56Z | - |
dc.date.issued | 2018 | |
dc.identifier.issn | 00278424 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/14356 | - |
dc.description.abstract | Iron chronically limits aquatic photosynthesis, especially in marine environments, and the correct perception and maintenance of iron homeostasis in photosynthetic bacteria, including cyanobacteria, is therefore of global significance. Multiple adaptive mechanisms, responsive promoters, and posttranscriptional regulators have been identified, which allow cyanobacteria to respond to changing iron concentrations. However, many factors remain unclear, in particular, how iron status is perceived within the cell. Here we describe a cyanobacterial ferredoxin (Fed2), with a unique C-terminal extension, that acts as a player in iron perception. Fed2 homologs are highly conserved in photosynthetic organisms from cyanobacteria to higher plants, and, although they belong to the plant type ferredoxin family of [2Fe-2S] photosynthetic electron carriers, they are not involved in photosynthetic electron transport. As deletion of fed2 appears lethal, we developed a C-terminal truncation system to attenuate protein function. Disturbed Fed2 function resulted in decreased chlorophyll accumulation, and this was exaggerated in iron-depleted medium, where different truncations led to either exaggerated or weaker responses to low iron. Despite this, iron concentrations remained the same, or were elevated in all truncation mutants. Further analysis established that, when Fed2 function was perturbed, the classical iron limitation marker IsiA failed to accumulate at transcript and protein levels. By contrast, abundance of IsiB, which shares an operon with isiA, was unaffected by loss of Fed2 function, pinpointing the site of Fed2 action in iron perception to the level of posttranscriptional regulation. | |
dc.description.sponsorship | Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [HA5921/1-1]; BBSRCUK Research & Innovation (UKRI)Biotechnology and Biological Sciences Research Council (BBSRC) [BB/L013711/1, BB/K00817X/1] Funding Source: UKRI; We thank Professor Conrad Mullineaux (Queen Mary University of London) for helpful discussions and insight, Giulia Mastoianni (Queen Mary University of London) for excellent technical support in the production and interpretation of TEM images, and Werner Bigott (University of Freiburg) for isolation of RNA. We thank Nestor Carrillo (Rosario University) for the kind gift of the antibody against IsiB. We acknowledge funding from the Deutsche Forschungsgemeinschaft Grant HA5921/1-1 (to G.T.H.) for some of this work. | |
dc.language.iso | en | |
dc.publisher | NATL ACAD SCIENCES | |
dc.relation.ispartof | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | |
dc.subject | cyanobacteria | |
dc.subject | CYANOBACTERIUM | |
dc.subject | DEFICIENCY | |
dc.subject | ESCHERICHIA-COLI | |
dc.subject | EXPRESSION | |
dc.subject | FdC2 | |
dc.subject | fed2 | |
dc.subject | ferredoxin | |
dc.subject | FLUORESCENCE | |
dc.subject | iron | |
dc.subject | ISIAB OPERON | |
dc.subject | Multidisciplinary Sciences | |
dc.subject | PHOTOSYSTEM-I | |
dc.subject | PROTEIN | |
dc.subject | REDUCTION | |
dc.subject | Science & Technology - Other Topics | |
dc.subject | SP PCC 6803 | |
dc.title | A unique ferredoxin acts as a player in the low-iron response of photosynthetic organisms | |
dc.type | journal article | |
dc.identifier.doi | 10.1073/pnas.1810379115 | |
dc.identifier.isi | ISI:000453529800028 | |
dc.description.volume | 115 | |
dc.description.issue | 51 | |
dc.description.startpage | E12111-E12120 | |
dc.contributor.orcid | 0000-0001-5586-1092 | |
dc.contributor.orcid | 0000-0002-0251-9231 | |
dc.contributor.researcherid | J-6363-2012 | |
dc.contributor.researcherid | AAB-4516-2020 | |
dc.publisher.place | 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA | |
dcterms.isPartOf.abbreviation | Proc. Natl. Acad. Sci. U. S. A. | |
dcterms.oaStatus | Green Accepted, Green Published, hybrid | |
crisitem.author.dept | Institut für Chemie neuer Materialien | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | institute11 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.orcid | 0000-0002-5497-034X | - |
crisitem.author.orcid | 0000-0002-6140-6181 | - |
crisitem.author.parentorg | FB 05 - Biologie/Chemie | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.grandparentorg | Universität Osnabrück | - |
crisitem.author.netid | WaLo966 | - |
crisitem.author.netid | ScRe288 | - |
crisitem.author.netid | HaGu059 | - |
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