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The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase

Isabelle Landrieu, Lieven De Veylder UGent, Jean-Sébastien Fruchart, Benoît Odaert UGent, Peter Casteels UGent, Daniel Portetelle, Marc Van Montagu UGent, Dirk Inzé UGent and Guy Lippens UGent (2000) JOURNAL OF BIOLOGICAL CHEMISTRY. 275(14). p.10577-10581
abstract
A homologue of the human site-specific prolyl cis/trans isomerase PIN1 was identified in Arabidopsis thaliana. The PIN1At gene encodes a protein of 119 amino acids that is 53% identical with the catalytic domain of the human PIN1 parvulin. Steady-state PIN1At mRNA is found in all plant tissues tested. We show by two-dimensional NMR spectroscopy that the PIN1At is a prolyl cis/trans isomerase with specificity for phosphoserine-proline bonds. PIN1At is the first example of an eukaryotic parvulin without N- or C-terminal extensions. The N-terminal WW domain of 40 amino acids, typical of all the phosphorylation-dependent eukaryotic parvulins, is absent. However, triple-resonance NMR experiments showed that PIN1At contained a hydrophobic helix similar to the al helix observed in PIN1 that could mediate the protein-protein interactions.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
SUBSTRATE RECOGNITION, SACCHAROMYCES-CEREVISIAE, WW DOMAIN, PROTEIN, SEQUENCE, PHOSPHOPROTEINS, ISOMERIZATION, SPECTROSCOPY, CALCITONIN, PARVULIN
journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
J. Biol. Chem.
volume
275
issue
14
pages
10577 - 10581
Web of Science type
Article
Web of Science id
000086345600093
ISSN
0021-9258
DOI
10.1074/jbc.275.14.10577
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
124990
handle
http://hdl.handle.net/1854/LU-124990
date created
2004-01-14 13:36:00
date last changed
2016-12-19 15:37:49
@article{124990,
  abstract     = {A homologue of the human site-specific prolyl cis/trans isomerase PIN1 was identified in Arabidopsis thaliana. The PIN1At gene encodes a protein of 119 amino acids that is 53\% identical with the catalytic domain of the human PIN1 parvulin. Steady-state PIN1At mRNA is found in all plant tissues tested. We show by two-dimensional NMR spectroscopy that the PIN1At is a prolyl cis/trans isomerase with specificity for phosphoserine-proline bonds. PIN1At is the first example of an eukaryotic parvulin without N- or C-terminal extensions. The N-terminal WW domain of 40 amino acids, typical of all the phosphorylation-dependent eukaryotic parvulins, is absent. However, triple-resonance NMR experiments showed that PIN1At contained a hydrophobic helix similar to the al helix observed in PIN1 that could mediate the protein-protein interactions.},
  author       = {Landrieu, Isabelle and De Veylder, Lieven and Fruchart, Jean-S{\'e}bastien and Odaert, Beno{\^i}t and Casteels, Peter and Portetelle, Daniel and Van Montagu, Marc and Inz{\'e}, Dirk and Lippens, Guy},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keyword      = {SUBSTRATE RECOGNITION,SACCHAROMYCES-CEREVISIAE,WW DOMAIN,PROTEIN,SEQUENCE,PHOSPHOPROTEINS,ISOMERIZATION,SPECTROSCOPY,CALCITONIN,PARVULIN},
  language     = {eng},
  number       = {14},
  pages        = {10577--10581},
  title        = {The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase},
  url          = {http://dx.doi.org/10.1074/jbc.275.14.10577},
  volume       = {275},
  year         = {2000},
}

Chicago
Landrieu, Isabelle, Lieven De Veylder, Jean-Sébastien Fruchart, Benoît Odaert, Peter Casteels, Daniel Portetelle, Marc Van Montagu, Dirk Inzé, and Guy Lippens. 2000. “The Arabidopsis Thaliana PIN1At Gene Encodes a Single-domain Phosphorylation-dependent Peptidyl Prolyl Cis/trans Isomerase.” Journal of Biological Chemistry 275 (14): 10577–10581.
APA
Landrieu, I., De Veylder, L., Fruchart, J.-S., Odaert, B., Casteels, P., Portetelle, D., Van Montagu, M., et al. (2000). The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase. JOURNAL OF BIOLOGICAL CHEMISTRY, 275(14), 10577–10581.
Vancouver
1.
Landrieu I, De Veylder L, Fruchart J-S, Odaert B, Casteels P, Portetelle D, et al. The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase. JOURNAL OF BIOLOGICAL CHEMISTRY. 2000;275(14):10577–81.
MLA
Landrieu, Isabelle, Lieven De Veylder, Jean-Sébastien Fruchart, et al. “The Arabidopsis Thaliana PIN1At Gene Encodes a Single-domain Phosphorylation-dependent Peptidyl Prolyl Cis/trans Isomerase.” JOURNAL OF BIOLOGICAL CHEMISTRY 275.14 (2000): 10577–10581. Print.