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The transcription regulator RbsR represents a novel interaction partner of the phosphoprotein HPr‐Ser46‐P in Bacillus subtilis
Author(s) -
Müller Wolfgang,
Horstmann Nicola,
Hillen Wolfgang,
Sticht Heinrich
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05148.x
Subject(s) - catabolite repression , ccpa , pep group translocation , bacillus subtilis , lac repressor , repressor , operon , lac operon , biochemistry , psychological repression , transcriptional regulation , derepression , regulator , biology , transcription (linguistics) , chemistry , genetics , transcription factor , gene , bacteria , escherichia coli , gene expression , linguistics , philosophy , mutant
Histidine‐containing protein (HPr) is a central metabolic sensor in low‐GC Gram‐positive bacteria and plays a dual role in sugar uptake by the phosphoenolpyruvate–sugar phosphotransferase system and in transcriptional control during carbon catabolite repression. The latter process is mediated by interaction between HPr and the carbon catabolite repression master transcription regulator, carbon catabolite protein A (CcpA), a member of the LacI‐GalR family of DNA‐binding proteins. We investigated, with a combination of computational and experimental tools, whether HPr can also interact with other transcriptional regulators. To allow rapid identification of paralogous LacI‐GalR family members that might interact with HPr in a similar fashion to CcpA, a structure‐based computational approach was developed which relies on the analysis of the similarity of protein–protein interfaces between different complexes. A key element of this method is an empirical pair potential derived from a group of orthologous complexes and subsequently used to identify paralogs that exhibit similar properties of their protein interfaces. Application of this method to the family of LacI‐GalR repressors in Bacillus subtilis predicted the ribose operon repressor (RbsR) as a novel interaction partner of HPr. This interaction was subsequently confirmed experimentally and suggests that HPr plays an even larger role in transcriptional control than previously expected.