Regulation of virulence by members of the MarR/SlyA family

• Published in: Current opinion in microbiology 2006-04, Vol.9 (2), p.153-159
• Main Authors: Ellison, Damon W, Miller, Virginia L
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Cyclic AMP Receptor Protein - metabolism; DNA-Binding Proteins - metabolism; DNA-Directed RNA Polymerases - metabolism; Gene Expression Regulation, Bacterial; Molecular Sequence Data; Pectobacterium chrysanthemi - genetics; Pectobacterium chrysanthemi - metabolism; Pectobacterium chrysanthemi - pathogenicity; Regulon; Repressor Proteins - genetics; Repressor Proteins - metabolism; Salmonella - genetics; Salmonella - metabolism; Salmonella - pathogenicity; Sequence Alignment; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism; Virulence; Yersinia - genetics; Yersinia - metabolism; Yersinia - pathogenicity
• ISSN: 1369-5274; 1879-0364
• DOI: 10.1016/j.mib.2006.02.003

Virulence gene regulators RovA, SlyA and PecS comprise a subset of the MarR/SlyA family of transcriptional regulators, which has been shown to be involved in the regulation of virulence genes. These regulators have all been shown to both positively and negatively regulate the expression of multiple genes, involving several different mechanisms. One of the conserved mechanisms of regulatory control among these proteins appears to be competition for binding sites with other proteins. SlyA negatively regulates its own expression by interfering with the binding of RNA polymerase, whereas RovA appears to interfere with the progression of RNA polymerase from its promoter and to compete for binding with the heat-stable nucleoid-structural protein (H-NS), a global transcriptional silencer. PecS represses transcription by competing for binding with cAMP receptor protein, a global activator. RovA, SlyA and PecS have all been shown to act as derepressors by competing for binding sites with repressors. Recently, RovA also was found to enhance transcription through interaction with RNA polymerase.