Cardiolipin synthase is required for Streptomyces coelicolor morphogenesis

Vinod Jyothikumar, Khanungkan Klanbut, John Tiong, James S. Roxburgh, Iain S. Hunter, Terry K. Smith, Paul R. Herron

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The fluid mosaic model has recently been amended to account for the existence of membrane domains enriched in certain phospholipids. In rod-shaped bacteria, the anionic phospholipid cardiolipin is enriched at the cell poles but its role in the morphogenesis of the filamentous bacterium Streptomyces coelicolor is unknown. It was impossible to delete clsA (cardiolipin synthase; SCO1389) unless complemented by a second copy of clsA elsewhere in the chromosome. When placed under the control of an inducible promoter, clsA expression, phospholipid profile and morphogenesis became inducer dependent. TLC analysis of phospholipid showed altered profiles upon depletion of clsA expression. Analysis of cardiolipin by mass spectrometry showed two distinct cardiolipin envelopes that reflected differences in acyl chain length; the level of the larger cardiolipin envelope was reduced in concert with clsA expression. ClsA-EGFP did not localize to specific locations, but cardiolipin itself showed enrichment at hyphal tips, branch points and anucleate regions. Quantitative analysis of hyphal dimensions showed that the mycelial architecture and the erection of aerial hyphae were affected by the expression of clsA. Overexpression of clsA resulted in weakened hyphal tips, misshaped aerial hyphae and anucleate spores and demonstrates that cardiolipin synthesis is a requirement for morphogenesis in Streptomyces.

Original languageEnglish
Pages (from-to)181-197
Number of pages17
JournalMolecular Microbiology
Volume84
Issue number1
Early online date13 Mar 2012
DOIs
Publication statusPublished - 1 Apr 2012

Keywords

  • fluid mosaic model
  • phospholipids
  • Streptomyces coelicolor
  • mycelial architecture

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