Both activity and expression of (ADP-ribosyl)ating proteins were tested in cells at different growth phases of Alicyclobacillus, Bacillus and Thermus genera, thermophilic and aerobic bacteria, isolated from different geothermal sources. An active (ADP-ribosyl)ating system was demonstrated in all analyzed microorganisms, with comparable enzymatic levels. Immunochemical analyses with polyclonal antibodies against both eukaryotic anti-(ADP-ribose) transferase and anti-poly(ADP-ribose) polymerase revealed, for all tested organisms, an immunosignal localized in the range of molecular masses between 43–53 kD. Several proteins of various molecular masses were found as ADP-ribose acceptors. Reaction product analysesshowed mono(ADP-ribose) to be the only synthesized compound.
The (ADP-ribosyl)ation reaction in thermophilic bacteria / FARAONE MENNELLA, MARIA ROSARIA; DE MAIO, Anna; A., Petrella; M., Romano; P., Favaloro; A., Gambacorta; L., Lama; B., Nicolaus; Farina, Benedetta. - In: RESEARCH IN MICROBIOLOGY. - ISSN 0923-2508. - ELETTRONICO. - 157:(2006), pp. 531-537.
The (ADP-ribosyl)ation reaction in thermophilic bacteria
FARAONE MENNELLA, MARIA ROSARIA;DE MAIO, ANNA;FARINA, BENEDETTA
2006
Abstract
Both activity and expression of (ADP-ribosyl)ating proteins were tested in cells at different growth phases of Alicyclobacillus, Bacillus and Thermus genera, thermophilic and aerobic bacteria, isolated from different geothermal sources. An active (ADP-ribosyl)ating system was demonstrated in all analyzed microorganisms, with comparable enzymatic levels. Immunochemical analyses with polyclonal antibodies against both eukaryotic anti-(ADP-ribose) transferase and anti-poly(ADP-ribose) polymerase revealed, for all tested organisms, an immunosignal localized in the range of molecular masses between 43–53 kD. Several proteins of various molecular masses were found as ADP-ribose acceptors. Reaction product analysesshowed mono(ADP-ribose) to be the only synthesized compound.| File | Dimensione | Formato | |
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