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  • Fekry, MostafaCairo University,Lund University (författare)

SAXS and stability studies of iron-induced oligomers of bacterial frataxin CyaY

  • Artikel/kapitelEngelska2017

Förlag, utgivningsår, omfång ...

  • 2017-09-20
  • Public Library of Science (PLoS),2017

Nummerbeteckningar

  • LIBRIS-ID:oai:lup.lub.lu.se:6b8bbe9b-625f-43cb-bff2-372dd867b3dd
  • https://lup.lub.lu.se/record/6b8bbe9b-625f-43cb-bff2-372dd867b3ddURI
  • https://doi.org/10.1371/journal.pone.0184961DOI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:art swepub-publicationtype
  • Ämneskategori:ref swepub-contenttype

Anmärkningar

  • Frataxin is a highly conserved protein found in both prokaryotes and eukaryotes. It is involved in several central functions in cells, which include iron delivery to biochemical processes, such as heme synthesis, assembly of iron-sulfur clusters (ISC), storage of surplus iron in conditions of iron overload, and repair of ISC in aconitase. Frataxin from different organisms has been shown to undergo iron-dependent oligomerization. At least two different classes of oligomers, with different modes of oligomer packing and stabilization, have been identified. Here, we continue our efforts to explore the factors that control the oligomerization of frataxin from different organisms, and focus on E. coli frataxin CyaY. Using small-angle X-ray scattering (SAXS), we show that higher iron-to-protein ratios lead to larger oligomeric species, and that oligomerization proceeds in a linear fashion as a results of iron oxidation. Native mass spectrometry and online size-exclusion chromatography combined with SAXS show that a dimer is the most common form of CyaY in the presence of iron at atmospheric conditions. Modeling of the dimer using the SAXS data confirms the earlier proposed head-to-tail packing arrangement of monomers. This packing mode brings several conserved acidic residues into close proximity to each other, creating an environment for metal ion binding and possibly even mineralization. Together with negative-stain electron microscopy, the experiments also show that trimers, tetramers, pentamers, and presumably higher-order oligomers may exist in solution. Nano-differential scanning fluorimetry shows that the oligomers have limited stability and may easily dissociate at elevated temperatures. The factors affecting the possible oligomerization mode are discussed.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Alshokry, WessenLund University (författare)
  • Grela, PrzemysławMaria Curie-Skłodowska University (författare)
  • Tchórzewski, MarekMaria Curie-Skłodowska University(Swepub:lu)mbfy-mtc (författare)
  • Ahlgren, Eva ChristinaLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)mbfy-eca (författare)
  • Söderberg, Christopher A.Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory(Swepub:lu)mbfy-ces (författare)
  • Gakh, OleksandrMayo Clinic Minnesota (författare)
  • Isaya, GraziaMayo Clinic Minnesota (författare)
  • Al-Karadaghi, SalamLund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH(Swepub:lu)mbfys-sa (författare)
  • Cairo UniversityLund University (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:PLoS ONE: Public Library of Science (PLoS)12:9, s. 0184961-01849611932-6203

Internetlänk

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  • PLoS ONE (Sök värdpublikationen i LIBRIS)

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