engleski

Macrodomain protein from bacterium Streptomyces coelicolor

Macrodomains are evolutionary conserved structural domains that bind ADP-ribose derivatives found in proteins with diverse cellular functions. Some proteins from the macrodomain family (human MacroD1, MacroD2) can hydrolyze ADP-ribosylated substrates and therefore reverse posttranslational modification - ADP-ribosylation in which an ADP-ribose moiety from NAD+ is transferred to a target protein. ADP-ribosylation can alter the physical and chemical properties of target proteins and controls many important cellular processes. Bacteria, and Streptomyces in particular, are known to utilize protein ADP- ribosylation to control a variety of important pathways (such as morphological differentiation and antibiotic production). We have determined crystal structure and biochemically and functionally characterized a macrodomain protein form bacterium Streptomyces coelicolor. This protein is a member of an uncharacterised subfamily of macrodomain proteins. Its crystal structure revealed highly conserved macrodomain fold. This macrodomain protein is involved in the DNA damage response, while knockout strain shows a conditional effect on antibiotic production. Our results give us a first insight into the molecular basis of its action, involvement in ADP-ribosylation cycle and impact on Streptomyces metabolism.

DNA damage response ; Macrodomain ; Poly(ADP‐ribose)

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