Loop mutations affect ferritin solubility causing non-native aggregation of subunits or precipitation of fully assembled polymers

Roberto Jappelli, Gianni Cesareni

Research output: Contribution to journalArticle

Abstract

As a consequence of elevated expression rates, the intracellular aggregation of polypeptide chains is commonly observed in E. coli. Although wild-type human ferritin, a polymeric iron storage protein, accumulates in the soluble form at high level in the bacterial cytoplasmic fraction, some amino acid substitutions in an exposed loop direct the synthesis of a highly insoluble product. We found that two mechanisms can lead to the aggregation of ferritin. While some mutations prevent ferritin polymerisation, others cause the precipitation of molecules in the assembled state.

Original languageEnglish
Pages (from-to)311-315
Number of pages5
JournalFEBS Letters
Volume394
Issue number3
DOIs
Publication statusPublished - Oct 7 1996

Keywords

  • Aggregation
  • Ferritin
  • Inclusion body
  • Loop
  • Protein assembly
  • Protein folding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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