| dc.contributor.author |
Dimou, M |
en |
| dc.contributor.author |
Zografou, C |
en |
| dc.contributor.author |
Venieraki, A |
en |
| dc.contributor.author |
Katinakis, P |
en |
| dc.date.accessioned |
2014-06-06T06:51:49Z |
|
| dc.date.available |
2014-06-06T06:51:49Z |
|
| dc.date.issued |
2012 |
en |
| dc.identifier.issn |
0006291X |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/j.bbrc.2012.07.021 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/5717 |
|
| dc.subject |
Acetyl-CoA carboxylase |
en |
| dc.subject |
Biotin carboxylase |
en |
| dc.subject |
CoA |
en |
| dc.subject |
Cyclophilin |
en |
| dc.subject |
Peptidyl-prolyl cis/trans isomerase |
en |
| dc.subject |
PPIase |
en |
| dc.subject |
Protein interaction |
en |
| dc.subject.other |
acetyl coenzyme A carboxylase |
en |
| dc.subject.other |
biotin carboxylase |
en |
| dc.subject.other |
biotin derivative |
en |
| dc.subject.other |
cyclophilin |
en |
| dc.subject.other |
fatty acid |
en |
| dc.subject.other |
unclassified drug |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
catalysis |
en |
| dc.subject.other |
controlled study |
en |
| dc.subject.other |
cytoplasm |
en |
| dc.subject.other |
enzyme activity |
en |
| dc.subject.other |
enzyme binding |
en |
| dc.subject.other |
fatty acid synthesis |
en |
| dc.subject.other |
hydrolysis kinetics |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
priority journal |
en |
| dc.subject.other |
protein interaction |
en |
| dc.subject.other |
Acetyl-CoA Carboxylase |
en |
| dc.subject.other |
Adenosine Triphosphate |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
Bacterial Proteins |
en |
| dc.subject.other |
Carbon-Nitrogen Ligases |
en |
| dc.subject.other |
Cyclophilins |
en |
| dc.subject.other |
Cytoplasm |
en |
| dc.subject.other |
Hydrolysis |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
Bacteria (microorganisms) |
en |
| dc.title |
Functional interaction of Azotobacter vinelandii cytoplasmic cyclophilin with the biotin carboxylase subunit of acetyl-CoA carboxylase |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/j.bbrc.2012.07.021 |
en |
| heal.publicationDate |
2012 |
en |
| heal.abstract |
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. © 2012 Elsevier Inc. |
en |
| heal.journalName |
Biochemical and Biophysical Research Communications |
en |
| dc.identifier.issue |
4 |
en |
| dc.identifier.volume |
424 |
en |
| dc.identifier.doi |
10.1016/j.bbrc.2012.07.021 |
en |
| dc.identifier.spage |
736 |
en |
| dc.identifier.epage |
739 |
en |