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Volume 164, Issue 4

Three novel proteins co-localise with polyhydroxybutyrate (PHB) granules in S1 Free

Abstract

Polyhydroxybutyrate (PHB), a biodegradable polymer accumulated by bacteria is deposited intracellularly in the form of inclusion bodies often called granules. The granules are supramolecular complexes harbouring a varied number of proteins on their surface, which have specific but incompletely characterised functions. By comparison with other organisms that produce biodegradable polymers, only two phasins have been described to date for raising the possibility that more await discovery. Using a comparative proteomics strategy to compare the granules of wild-type with a PHB-negative mutant housing artificial PHB granules, we identified four potential PHB granules’ associated proteins. These were: Q2RSI4, an uncharacterised protein; Q2RWU9, annotated as an extracellular solute-binding protein; Q2RQL4, annotated as basic membrane lipoprotein; and Q2RQ51, annotated as glucose-6-phosphate isomerase. analysis revealed that Q2RSI4 harbours a family domain and shares low identity with a single-strand DNA-binding protein from . Fluorescence microscopy found that three proteins Q2RSI4, Q2EWU9 and Q2RQL4 co-localised with PHB granules. This work adds three potential new granule associated proteins to the repertoire of factors involved in bacterial storage granule formation, and confirms that proteomics screens are an effective strategy for discovery of novel granule associated proteins.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): comparative proteomics , confocal microscopy , phasins , polyhydroxybutyrate PHB and Rhodospirillum rubrum
© 2018 The Authors
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2018-04-01
2024-04-20
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Three novel proteins co-localise with polyhydroxybutyrate (PHB) granules in Rhodospirillum rubrum S1
Microbiology 164, 625 (2018); https://doi.org/10.1099/mic.0.000642
/content/journal/micro/10.1099/mic.0.000642
/content/journal/micro/10.1099/mic.0.000642
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