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The transcription regulator RbsR represents a novel interaction partner of the phosphoprotein Hpr-Ser46-P in Bacillus subtilis

Authors: Wolfgang Müller, Nicola Horstmann, Wolfgang Hillen, and Heinrich Sticht

Field: Biochemistry, Bioinformatics, Microbiology

Document Content: This study investigates the interaction between the histidine-containing protein (HPr) and transcriptional regulators in Bacillus subtilis. Using a structure-based computational approach combined with experimental validation, the research identifies the ribose operon repressor (RbsR) as a novel interaction partner of HPr, specifically the phosphorylated form HPr-Ser46-P. This finding suggests a broader role for HPr in transcriptional control than previously understood, participating in carbon catabolite repression alongside CcpA.

Detailed Table of Contents:

  • Keywords
  • Correspondence
  • Abstract
  • Introduction (Histidine-containing protein (HPr), Carbon catabolite repression, CcpA, HPr-Ser46-P)
  • Abbreviations
  • Prediction of novel protein-protein interactions
  • Results and Discussion
  • General outline of the approach used to identify novel protein-protein interactions
  • Molecular modeling and interface analysis of the orthologous complexes
  • Molecular modeling and interface analysis of the paralogous complexes
  • RbsR as a novel interaction partner for HPr-Ser46-P
  • Structural comparison of the HPr-CcpA and HPr-RbsR complexes
  • Conclusions
  • Experimental procedures
  • Sequence search and molecular modeling
  • Scoring of the protein-protein interfaces
  • Cloning
  • Protein purification
  • EMSA
  • Acknowledgements
  • References
  • Supplementary material