World Library  

Add to Book Shelf
Flag as Inappropriate
Email this Book

Plos Biology : Structural Basis of Response Regulator Inhibition by a Bacterial Anti-activator Protein, Volume 9

By Stock, Ann

Click here to view

Book Id: WPLBN0003952314
Format Type: PDF eBook :
File Size:
Reproduction Date: 2015

Title: Plos Biology : Structural Basis of Response Regulator Inhibition by a Bacterial Anti-activator Protein, Volume 9  
Author: Stock, Ann
Volume: Volume 9
Language: English
Subject: Journals, Science, Biology
Collections: Periodicals: Journal and Magazine Collection, PLoS Biology
Publication Date:
Publisher: Plos


APA MLA Chicago

Stock, A. (n.d.). Plos Biology : Structural Basis of Response Regulator Inhibition by a Bacterial Anti-activator Protein, Volume 9. Retrieved from

Description : The complex interplay between the response regulator ComA, the anti-activator RapF, and the signaling peptide PhrF controls competence development in Bacillus subtilis. More specifically, ComA drives the expression of genetic competence genes, while RapF inhibits the interaction of ComA with its target promoters. The signaling peptide PhrF accumulates at high cell density and upregulates genetic competence by antagonizing the interaction of RapF and ComA. How RapF functions mechanistically to inhibit ComA activity and how PhrF in turn antagonizes the RapF-ComA interaction were unknown. Here we present the X-ray crystal structure of RapF in complex with the ComA DNA binding domain. Along with biochemical and genetic studies, the X-ray crystal structure reveals how RapF mechanistically regulates ComA function. Interestingly, we found that a RapF surface mimics DNA to block ComA binding to its target promoters. Furthermore, RapF is a monomer either alone or in complex with PhrF, and it undergoes a conformational change upon binding to PhrF, which likely causes the dissociation of ComA from the RapF-ComA complex. Finally, we compare the structure of RapF complexed with the ComA DNA binding domain and the structure of RapH complexed with Spo0F. This comparison reveals that RapF and RapH have strikingly similar overall structures, and that they have evolved different, non-overlapping surfaces to interact with diverse cellular targets. To our knowledge, the data presented here reveal the first atomic level insight into the inhibition of response regulator DNA binding by an anti-activator. Compounds that affect the interaction of Rap and Raplike proteins with their target domains could serve to regulate medically and commercially important phenotypes in numerous Bacillus species, such as sporulation in B. anthracis and sporulation and the production of Cry protein endotoxin in B. Thuringiensis.


Click To View

Additional Books

  • Plos Biology : Binding of Superantigen T... (by )
  • Plos Biology : Anthranilate Fluorescence... (by )
  • Plos Biology : Electrostatically Biased ... (by )
  • Plos Biology : the Circadian Clock Coord... (by )
  • Plos Biology : the Foxa2 Gene Controls t... (by )
  • Plos Biology : Global Conformational Dyn... (by )
  • Plos Biology : Reduction of the Choleste... (by )
  • Plos Biology : Eco-defense Against Invas... (by )
  • Plos Biology : Binding Site Turnover Pro... (by )
  • Plos Biology : Identifying Genes That He... (by )
  • Plos Biology : Interdependency of Brassi... (by )
  • Plos Biology : the Implications of Multi... (by )
Scroll Left
Scroll Right


Copyright © World Library Foundation. All rights reserved. eBooks from World Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.