Scientists have captured the first “snapshot” of two proteins involved in delivering a bacterial stress-response master regulator to the cell’s recycling machinery.
Scientists have captured the first “snapshot” of two proteins involved in delivering a bacterial stress-response master regulator to the cell’s recycling machinery.
The Brown University-led team found that RssB — a protein that specifically recognizes the master regulator and delivers it to the recycling machinery somewhat like a recycling truck — forms a compact structure with a factor that inhibits RssB activity. The inhibition factor, called IraD, is triggered by DNA damage, one of many stresses the master regulator helps bacteria survive by turning on important genes.
The stress-response master regulator is critical for many bacteria — including those that cause human disease such as E. coli and Salmonella — to survive nutrient deprivation and other stressful situations such as those encountered during the process of infecting a new host. It is also important for the development and growth of biofilms, which are often resistant to antibiotics and grow on medical devices such as catheters and artificial heart valves.
Read more at Brown University
Image: A false-color structure of RssB (pink and cyan) — a protein that specifically recognizes a critical stress-response master regulator in bacteria and delivers it to the recycling machinery somewhat like a recycling truck — bound to IraD (green) — a factor that inhibits RssB activity. Both lobes of RssB, which are connected by a flexible linker (magenta) contact IraD in a “hug.” Image courtesy Alexandra Deaconescu.
