| dc.contributor.author |
Dimou, M |
en |
| dc.contributor.author |
Venieraki, A |
en |
| dc.contributor.author |
Zografou, C |
en |
| dc.contributor.author |
Katinakis, P |
en |
| dc.date.accessioned |
2014-06-06T06:52:08Z |
|
| dc.date.available |
2014-06-06T06:52:08Z |
|
| dc.date.issued |
2012 |
en |
| dc.identifier.issn |
03014851 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1007/s11033-011-1196-1 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/5862 |
|
| dc.subject |
Cyclophilin |
en |
| dc.subject |
Peptidyl-prolyl cis/trans isomerase |
en |
| dc.subject |
Phosphate acetyltransferase |
en |
| dc.subject |
Protein interaction |
en |
| dc.subject.other |
cyclophilin |
en |
| dc.subject.other |
isoenzyme |
en |
| dc.subject.other |
peptidylprolyl isomerase |
en |
| dc.subject.other |
phosphate acetyltransferase |
en |
| dc.subject.other |
PTA 1 protein |
en |
| dc.subject.other |
PTA 2 protein |
en |
| dc.subject.other |
unclassified drug |
en |
| dc.subject.other |
bacterial protein |
en |
| dc.subject.other |
cyclophilin B |
en |
| dc.subject.other |
isoenzyme |
en |
| dc.subject.other |
isoprotein |
en |
| dc.subject.other |
mutant protein |
en |
| dc.subject.other |
phosphate acetyltransferase |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
bioinformatics |
en |
| dc.subject.other |
catalysis |
en |
| dc.subject.other |
down regulation |
en |
| dc.subject.other |
enzyme activation |
en |
| dc.subject.other |
enzyme active site |
en |
| dc.subject.other |
enzyme activity |
en |
| dc.subject.other |
enzyme assay |
en |
| dc.subject.other |
enzyme regulation |
en |
| dc.subject.other |
enzyme substrate complex |
en |
| dc.subject.other |
in vitro study |
en |
| dc.subject.other |
in vivo study |
en |
| dc.subject.other |
nonhuman |
en |
| dc.subject.other |
protein expression |
en |
| dc.subject.other |
protein protein interaction |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
cytoplasm |
en |
| dc.subject.other |
enzyme specificity |
en |
| dc.subject.other |
enzymology |
en |
| dc.subject.other |
metabolism |
en |
| dc.subject.other |
polyacrylamide gel electrophoresis |
en |
| dc.subject.other |
protein binding |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
Bacterial Proteins |
en |
| dc.subject.other |
Cyclophilins |
en |
| dc.subject.other |
Cytoplasm |
en |
| dc.subject.other |
Electrophoresis, Polyacrylamide Gel |
en |
| dc.subject.other |
Isoenzymes |
en |
| dc.subject.other |
Mutant Proteins |
en |
| dc.subject.other |
Phosphate Acetyltransferase |
en |
| dc.subject.other |
Protein Binding |
en |
| dc.subject.other |
Protein Isoforms |
en |
| dc.subject.other |
Substrate Specificity |
en |
| dc.title |
The cytoplasmic cyclophilin from Azotobacter vinelandii interacts with phosphate acetyltransferase isoforms enhancing their in vitro activity |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1007/s11033-011-1196-1 |
en |
| heal.publicationDate |
2012 |
en |
| heal.abstract |
Cyclophilins belong to the peptidyl-prolyl cis/ trans isomerase family of enzymes (EC 5.2.1.8), which accelerate protein folding by catalysing the cis/trans isomerisation of proline imidic peptide bonds. In the present study, by a combination of bioinformatics methods, we identify phosphate acetyltransferase isoforms, AvPTA-1 and AvPTA-2, as potential interacting partners of AvPPIB, the cytoplasmic cyclophilin from Azotobacter vinelandii, and demonstrate their physical interaction by co-expression studies. A decrease in AvPPIB PPIase activity, in the presence of AvPTA-1 or AvPTA-2, further confirms each interaction. Phosphate acetyltransferases (EC 2.3.1.8) catalyse the reversible transfer of the acetyl group from acetyl-P to CoA, forming acetyl-CoA and inorganic phosphate. We examined the effect of AvPPIB on the enzymatic activity of both phosphate acetyltransferase isoforms, and noticed an enhancement of the activity, as well as an alteration of the Km of each isoform, for the reaction substrates, indicating a possible function of AvPPIB in phosphate acetyltransferase activity modulation. Although PPIase activity seems not to be essential for these interactions, since AvPPIBF99A active site mutant still interacts with both isoforms, it is responsible for the observed phosphate acetyltransferase activity enhancement as AvPPIBF99A enhanced to a significantly lower extent the phosphate acetyltransferase activity of both isoforms compared with AvPPIB. © Springer Science+Business Media B.V. 2011. |
en |
| heal.journalName |
Molecular Biology Reports |
en |
| dc.identifier.issue |
4 |
en |
| dc.identifier.volume |
39 |
en |
| dc.identifier.doi |
10.1007/s11033-011-1196-1 |
en |
| dc.identifier.spage |
4135 |
en |
| dc.identifier.epage |
4143 |
en |