Thesis

Investigating the protein-protein interactions of SCO3607 and SCO3608 and their role in cell morphology in Streptomyces coelicolor

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Awarding institution
  • University of Strathclyde
Date of award
  • 2018
Thesis identifier
  • T14900
Person Identifier (Local)
  • 201080153
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Department, School or Faculty
Abstract
  • Flotillin is a protein intrinsic to cell viability in humans, where it plays a role in cell morphology and structure. In Bacillus subtilis, it is involved in sporulation. NfeD always accompanies flotillins in prokaryotes, normally as an adjacent gene, though it is not present in eukaryotes. SCO3607 and SCO3608, encoding flotillin and NfeD, respectively, are present in Streptomyces coelicolor. No previous studies have examined the role of these two proteins in S. coelicolor. Preliminary bioinformatics revealed NfeD-encoding genes in actinobacteria, which was tentatively suggested as a new group of NfeD proteins; NfeD1b-5. Tn5062 transposon insertions in SCO3607 and deletions of both genes, separately and together, displayed no macroscopic phenotype; while fluorescence microscopy revealed phenotypes related to cell polarity. SCO3607 mutants displayed shorter tip to branch and cross-wall to cross-wall distances, while SCO3608 mutants displayeda milder phenotype. A double knockout mutant displayed shorter intra cross-wall distances and enlarged spores. Bacterial two hybrid experiments were also performed, revealing SCO3607-SCO3607 interactions, though N-terminal fusions of the cya-domains to SCO3607 abolished the interaction, suggesting the N-terminus is essential for the interaction.
Advisor / supervisor
  • Herron, Paul
Resource Type
DOI
Date Created
  • 2018
Former identifier
  • 9912606193102996

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