کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1929072 | 1050443 | 2012 | 4 صفحه PDF | دانلود رایگان |
Cyclophilins (E.C. 5.1.2.8) are protein chaperones with peptidyl-prolyl cis/trans isomerase activity (PPIase). In the present study, we demonstrate a physical interaction among AvppiB, encoding the cytoplasmic cyclophilin from the soil nitrogen-fixing bacterium Azotobacter vinelandii, and AvaccC, encoding the biotin carboxylase subunit of acetyl-CoA carboxylase, which catalyzes the committed step in long-chain fatty acid synthesis. A decrease in AvppiB PPIase activity, in the presence of AvaccC, further confirms the interaction. However, PPIase activity seems not to be essential for these interactions since a PPIase active site mutant of cyclophilin does not abolish the AvaccC binding. We further show that the presence of cyclophilin largely influences the measured ATP hydrolyzing activity of AvaccA in a way that is negatively regulated by the PPIase activity. Taken together, our data support a novel role for cyclophilin in regulating biotin carboxylase activity.
► The cytoplasmic cyclophilin AvppiB binds the biotin carboxylase AvaccC.
► The PPIase active site of AvppiB although involved is not essential for the binding.
► AvppiB significantly influences the ATP hydrolyzing activity of AvaccC.
► PPIase activity of AvppiB negatively regulates the AvppiB mediated enhancement of AvaccC activity.
Journal: Biochemical and Biophysical Research Communications - Volume 424, Issue 4, 10 August 2012, Pages 736–739