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N-terminal domains of plant poly(ADP-ribose) polymerases define their association with mitotic chromosomes

Elena Babiychuk UGent, Marc Van Montagu UGent and Sergei Kushnir UGent (2001) PLANT JOURNAL. 28(3). p.245-255
abstract
Poly(ADP-ribos)ylation is a reversible protein modification that in higher plants is catalyzed by two structurally different poly(ADP-ribose) polymerases, App and Zap. In vivo imaging of green-fluorescent protein (GPF) fusions showed that both Zap and App were associated with chromatin through the cell cycle progression. The in vivo behaviour of the App-GFP protein fusions can be attributed to the activity of two NASA motifs that mediate protein-protein interactions and nucleic acid binding. Expression of Zap deletion variants revealed that both Zn fingers and helix-turn-helix domains contributed to the association with chromosomes, whereas the localization in the nucleoplasm was mostly determined by the Zn fingers. The results highlight novel properties of protein sequences found in plant poly(ADP-ribose) polymerases and suggest important functions for this class of nuclear enzymes in chromosome dynamics.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
chromatin, poly(ADP-ribose) polymerase, chromosomes, green-fluorescent protein, red-fluorescent protein, plants, MOLECULAR NICK-SENSOR, TRANSCRIPTION FACTORS, BINDING DOMAIN, HELA-CELLS, SAF-A, DNA, PROTEIN, INVOLVEMENT, ACTIVATION, CDNA
journal title
PLANT JOURNAL
Plant J.
volume
28
issue
3
pages
245 - 255
Web of Science type
Article
Web of Science id
000172295700001
JCR category
PLANT SCIENCES
JCR impact factor
5.792 (2001)
JCR rank
5/134 (2001)
JCR quartile
1 (2001)
ISSN
0960-7412
DOI
10.1046/j.1365-313X.2001.01143.x
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
138561
handle
http://hdl.handle.net/1854/LU-138561
date created
2004-01-14 13:37:00
date last changed
2016-12-19 15:37:50
@article{138561,
  abstract     = {Poly(ADP-ribos)ylation is a reversible protein modification that in higher plants is catalyzed by two structurally different poly(ADP-ribose) polymerases, App and Zap. In vivo imaging of green-fluorescent protein (GPF) fusions showed that both Zap and App were associated with chromatin through the cell cycle progression. The in vivo behaviour of the App-GFP protein fusions can be attributed to the activity of two NASA motifs that mediate protein-protein interactions and nucleic acid binding. Expression of Zap deletion variants revealed that both Zn fingers and helix-turn-helix domains contributed to the association with chromosomes, whereas the localization in the nucleoplasm was mostly determined by the Zn fingers. The results highlight novel properties of protein sequences found in plant poly(ADP-ribose) polymerases and suggest important functions for this class of nuclear enzymes in chromosome dynamics.},
  author       = {Babiychuk, Elena and Van Montagu, Marc and Kushnir, Sergei},
  issn         = {0960-7412},
  journal      = {PLANT JOURNAL},
  keyword      = {chromatin,poly(ADP-ribose) polymerase,chromosomes,green-fluorescent protein,red-fluorescent protein,plants,MOLECULAR NICK-SENSOR,TRANSCRIPTION FACTORS,BINDING DOMAIN,HELA-CELLS,SAF-A,DNA,PROTEIN,INVOLVEMENT,ACTIVATION,CDNA},
  language     = {eng},
  number       = {3},
  pages        = {245--255},
  title        = {N-terminal domains of plant poly(ADP-ribose) polymerases define their association with mitotic chromosomes},
  url          = {http://dx.doi.org/10.1046/j.1365-313X.2001.01143.x},
  volume       = {28},
  year         = {2001},
}

Chicago
Babiychuk, Elena, Marc Van Montagu, and Sergei Kushnir. 2001. “N-terminal Domains of Plant poly(ADP-ribose) Polymerases Define Their Association with Mitotic Chromosomes.” Plant Journal 28 (3): 245–255.
APA
Babiychuk, E., Van Montagu, M., & Kushnir, S. (2001). N-terminal domains of plant poly(ADP-ribose) polymerases define their association with mitotic chromosomes. PLANT JOURNAL, 28(3), 245–255.
Vancouver
1.
Babiychuk E, Van Montagu M, Kushnir S. N-terminal domains of plant poly(ADP-ribose) polymerases define their association with mitotic chromosomes. PLANT JOURNAL. 2001;28(3):245–55.
MLA
Babiychuk, Elena, Marc Van Montagu, and Sergei Kushnir. “N-terminal Domains of Plant poly(ADP-ribose) Polymerases Define Their Association with Mitotic Chromosomes.” PLANT JOURNAL 28.3 (2001): 245–255. Print.