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TitleThe assembly rules guiding hetero-oligomeric bacterioferritin organization and their evolutionary signature.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 5, Page e2504561123, Year 2026
Publish dateFeb 3, 2026
AuthorsDaniel Stein / Bruno Jartoux / Shiran Dror / René Uebe / Tracy Chih-Ting Koubková-Yu / Ran Zalk / Anat Shahar / Raz Zarivach / Gabriel A Frank /
PubMed AbstractHomomeric and heteromeric protein complexes are ubiquitous across all domains of life. The evolutionary transition from homo- to hetero-oligomers by gene duplication and chain specialization is ...Homomeric and heteromeric protein complexes are ubiquitous across all domains of life. The evolutionary transition from homo- to hetero-oligomers by gene duplication and chain specialization is widespread, yet it entails challenging requirements for maintaining oligomerization and functionality. Chain specialization in ferritins, which occurs in bacteria, vertebrates, and plants, is a salient example of this phenomenon. In heteroferritins, the two essential functions, ferroxidase activity and electron transfer, are split between two specialized chain types. Many heteroferritins assemble into complexes with variable subunit ratios, implying the existence of assembly rules that balance compositional flexibility with structural constraints. Here, we identify the assembly rules governing the organization of the heterobacterioferritin from (MSR-1 Bfr) by analyzing its cryo-EM reconstructions. These rules consist of structural constraints that limit the number of possible arrangements and promote juxtaposition of the two, now separated functions. These constraints support compositional flexibility while preserving function, thereby providing resilience to stochastic variation in oligomer stoichiometry. Bioinformatic analysis revealed that the assembly rules identified in MSR-1 Bfr are widespread across the Bfr family and coevolved with chain specialization. Together, these findings support leading models of hetero-oligomer evolution and reveal the emergence of order-exerting mutations that shape the organization of multimeric protein complexes while conserving function.
External linksProc Natl Acad Sci U S A / PubMed:41609675 / PubMed Central
MethodsEM (single particle)
Resolution2.86 Å
Structure data

51772

9h1u

EMDB-51772, PDB-9h1u:
Cryo-EM structure of Heterooligomeric Bacterioferritin
Method: EM (single particle) / Resolution: 2.86 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-FE:
Unknown entry

Source
  • magnetospirillum gryphiswaldense msr-1 (magnetotactic)
KeywordsMETAL BINDING PROTEIN / Heterooligomer / Iron-storage protein / Heme binding / Octahedral

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