Analysis of Poly(3-hydroxybutyrate) granule-associated proteome in recombinant Escherichia coli

Mee Jung Han, Si Jae Park, Jeong Wook Lee, Byoung Hoon Min, Sang Yup Lee, Soo Jin Kim, Jong Shin Yoo

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12 Scopus citations


Poly(3-hydroxybutyrate) [P(3HB)] is a microbial polyester intracellularly accumulated as distinct granules in numerous microorganisms as an energy and carbon storage material. Recombinant Escherichia coli harboring the heterologous P(3HB) biosynthesis genes accumulates large amounts of P(3HB) granules, yet the granule-associated proteins have not been identified. Therefore, this study reports on an analysis of the P(3HB) granule-associated proteome in recombinant E. coli. Five proteins out of 7 spots identified were found to be involved in functions of translation, heat-stress responses, and P(3HB) biosynthesis. Two of the major granule-associated proteins, IbpA/B, which are already known to bind to recombinant proteins forming inclusion bodies in E. coli, were further analyzed. Immunoblotting and immunoelectron microscopic studies with IbpA/B antibodies clearly demonstrated the binding and localization of IbpA/B to P(3HB) granules. IbpA/B seemed to play an important role in recombinant E. coli producing P(3HB) by stabilizing the interface between the hydrophobic P(3HB) granules and the hydrophilic cytoplasm. Thus, IbpA/B were found to act like phasins in recombinant E. coli, as they are the major proteins bound to the P(3HB) granules, affect the morphology of the granules, and reduce the amount of cytosolic proteins bound to the P(3HB) granules.

Original languageEnglish
Pages (from-to)901-910
Number of pages10
JournalJournal of Microbiology and Biotechnology
Issue number6
StatePublished - Jun 2006


  • Escherichia coli
  • IbpA/B
  • P(3HB)
  • P(3HB) granule-associated proteome
  • Small heat-shock proteins


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