CcpN: a moonlighting protein regulating catabolite repression of gluconeogenic genes in Bacillus subtilis also affects cell length and interacts with DivIVA

• Published in: Canadian journal of microbiology Vol. 66; no. 12; pp. 723 - 732
• Main Authors: Sharma, Kusum, Sultana, Taranum, Dahms, Tanya E.S, Dillon, Jo-Anne R
• Format: Journal Article
• Language: English
• Published: 1840 Woodward Drive, Suite 1, Ottawa, ON K2C 0P7 NRC Research Press 01.12.2020; Canadian Science Publishing NRC Research Press
• Subjects: Arginine; Bacillus (Bacteria); Bacillus subtilis; Bacillus subtilis - cytology; Bacillus subtilis - genetics; Bacillus subtilis - metabolism; Bacteria; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Biosynthesis; Catabolite repression; Catabolite Repression - genetics; CcpN; Cell Cycle Proteins - metabolism; Deactivation; DivIVA; Elongation; Enterococcus; Enterococcus faecalis; Gene Expression Regulation, Bacterial - genetics; Gene silencing; Genes; Genetic aspects; Gluconeogenesis; Gluconeogenesis - genetics; Glucose; Glutathione; Glutathione transferase; Gram-positive bacteria; Homology; Inactivation; interaction protéine–protéine; Microbiological research; Protein-protein interactions; Proteins; protein–protein interaction; Ribonucleic acid; RNA; Transcription; Canada; Enterococcus faecalis; interaction protéine–protéine; protein–protein interaction; CcpN; DivIVA; Bacillus subtilis
• ISSN: 0008-4166; 1480-3275
• DOI: 10.1139/cjm-2020-0022

CcpN is a transcriptional repressor in Bacillus subtilis that binds to the promoter region of gapB and pckA, downregulating their expression in the presence of glucose. CcpN also represses sr1, which encodes a small noncoding regulatory RNA that suppresses the arginine biosynthesis gene cluster. CcpN has homologues in other Gram-positive bacteria, including Enterococcus faecalis. We report the interaction of CcpN with DivIVA of B. subtilis as determined using bacterial two-hybrid and glutathione S-transferase pull-down assays. Insertional inactivation of CcpN leads to cell elongation and formation of straight chains of cells. These findings suggest that CcpN is a moonlighting protein involved in both gluconeogenesis and cell elongation.