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A comprehensive proteomic analysis of totarol induced alterations in Bacillus subtilis by multipronged quantitative proteomics.

Authors
  • Reddy, Panga Jaipal
  • Ray, Sandipan
  • Sathe, Gajanan J
  • Gajbhiye, Akshada
  • Prasad, T S Keshava
  • Rapole, Srikanth
  • Panda, Dulal
  • Srivastava, Sanjeeva
Type
Published Article
Journal
Journal of proteomics
Publication Date
Jan 30, 2015
Volume
114
Pages
247–262
Identifiers
DOI: 10.1016/j.jprot.2014.10.025
PMID: 25464363
Source
Medline
Keywords
License
Unknown

Abstract

The exact mechanism of action of totarol is still unclear and further investigations are essential to identify the molecular/cellular targets of this potential antimicrobial agent. The present study demonstrates the application of differential proteome to decipher the mechanism of action and molecular targets of totarol in B. subtilis. Our quantitative proteome analysis revealed that totarol induced alterations in the expression levels of 139 proteins (1.5 fold change and ≥2 peptides) in B. subtilis. Findings obtained from this study indicate that totarol treatment leads to metabolic shutdown by repressing the major central metabolic dehydrogenases in B. subtilis. In addition, expression levels of universal chaperone proteins, heme biosynthesis, and ribosomal proteins were found to be altered, which caused the filamentation of the bacteria. To the best of our knowledge, this is the foremost inclusive investigation describing totarol induced alterations in B. subtilis proteome and diverse physiological processes. We anticipate that this in depth proteomic study may contribute to a better understanding of the mode of action of totarol and its primary molecular and cellular targets.

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