Iron–sulfur cluster reconstitution of spinach chloroplast Rieske protein requires a partially prefolded apoprotein

Gubernator, Beata; Króliczewski, Jarosław; Kallas, Toivo; Szczepaniak, Andrzej

doi:10.1016/j.bbapap.2005.12.013

Cited by 9 publications

(8 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Iron–sulfur cluster assembly can be achieved by chemical reconstitution as well, since iron–sulfur apo-proteins are able to spontaneously form iron–sulfur clusters in vitro when supplied with iron and sulfide under reducing conditions 1 , 43 , 57 . With this approach, started with apo-clMagR WT , we successfully reconstituted [3Fe–4S] cluster in clMagR protein, confirmed by UV–Vis absorption and CD spectrum result (Fig.…”

Section: Resultsmentioning

confidence: 99%

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Guo

Chen

et al. 2021

Sci Rep

View full text Add to dashboard Cite

Iron–sulfur clusters are essential cofactors found in all kingdoms of life and play essential roles in fundamental processes, including but not limited to respiration, photosynthesis, and nitrogen fixation. The chemistry of iron–sulfur clusters makes them ideal for sensing various redox environmental signals, while the physics of iron–sulfur clusters and its host proteins have been long overlooked. One such protein, MagR, has been proposed as a putative animal magnetoreceptor. It forms a rod-like complex with cryptochromes (Cry) and possesses intrinsic magnetic moment. However, the magnetism modulation of MagR remains unknown. Here in this study, iron–sulfur cluster binding in MagR has been characterized. Three conserved cysteines of MagR play different roles in iron–sulfur cluster binding. Two forms of iron–sulfur clusters binding have been identified in pigeon MagR and showed different magnetic properties: [3Fe–4S]-MagR appears to be superparamagnetic and has saturation magnetization at 5 K but [2Fe–2S]-MagR is paramagnetic. While at 300 K, [2Fe–2S]-MagR is diamagnetic but [3Fe–4S]-MagR is paramagnetic. Together, the different types of iron–sulfur cluster binding in MagR attribute distinguished magnetic properties, which may provide a fascinating mechanism for animals to modulate the sensitivity in magnetic sensing.

show abstract

Section: Resultsmentioning

confidence: 99%

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Guo

Chen

et al. 2021

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Upon cluster integration, further folding occurs, allowing the Rieske protein to attain a final native structure. 119 EPR techniques have helped to characterize the geometry and environment of Fe-S clusters within cyt b 6 f complex as well as its redox reactions. [120][121][122][123][124][125] Most of these studies were developed in cyanobacterial systems but data from spinach cyt b 6 f were also reported.…”

Section: Photosystem IImentioning

confidence: 99%

Transition metals in plant photosynthesis

2013

View full text Add to dashboard Cite

Transition metals are involved in essential biological processes in plants since they are cofactors of metalloproteins and also act as regulator elements. Particularly, plant chloroplasts are organelles with high transition metal ion demand because metalloproteins are involved in the photosynthetic electron transport chain. The transition metal requirement of photosynthetic organisms greatly exceeds that of non-photosynthetic organisms, and either metal deficiency or metal excess strongly impacts photosynthetic functions. In chloroplasts, the transition metal ion requirement needs a homeostasis network that strictly regulates metal uptake, chelation, trafficking and storage since under some conditions metals cause toxicity. This review gives an overview of the current understanding of main features concerning the role of copper (Cu), iron (Fe), manganese (Mn) and zinc (Zn) in plant photosynthesis as well as the mechanisms involved in their homeostasis within chloroplasts. The metalloproteins functioning in photosynthetic proteins of plants as well as those proteins participating in the metal transport and metal binding assembly are reviewed. Furthermore, the role of nickel (Ni) in artificial photosynthesis will be discussed.

show abstract

“…However, it is noteworthy that studies investigating disulfide bond-assisted folding in the Tat system have, thus far, only been performed on heterologous proteins or with Escherichia coli fusion proteins (1-3, 70, 71). Furthermore, spinach-derived Rieske proteins required a partially folded state to allow for co-factor insertion when expressed in E. coli (72). Our present study is the first to examine the Tat-dependent export of a single native protein, the Rieske protein QcrA of B. subtilis, which requires both cofactor binding and disulfide bond formation for its biological function.…”

Section: Discussionmentioning

confidence: 94%

Co-factor Insertion and Disulfide Bond Requirements for Twin-arginine Translocase-dependent Export of the Bacillus subtilis Rieske Protein QcrA

Goosens

Monteferrante

Dijl

2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background:The Rieske protein QcrA was recently shown to be exported by twin-arginine translocation (Tat) in Bacillus subtilis. Results: QcrA has disulfide bond and co-factor requirements for effective Tat-dependent translocation. Conclusion: A hierarchy exists between disulfide bonding and co-factor insertion in QcrA quality control and translocation. Significance: First studies on Tat-dependent translocation where oxidative folding and co-factor attachment were addressed in a single native molecule.

show abstract

Iron–sulfur cluster reconstitution of spinach chloroplast Rieske protein requires a partially prefolded apoprotein

Cited by 9 publications

References 52 publications

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Modulation of MagR magnetic properties via iron–sulfur cluster binding

Transition metals in plant photosynthesis

Co-factor Insertion and Disulfide Bond Requirements for Twin-arginine Translocase-dependent Export of the Bacillus subtilis Rieske Protein QcrA

Contact Info

Product

Resources

About