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פותח על ידי קלירמאש פתרונות בע"מ -
Suppression and overexpression of ubiquitin extension protein S27a affects cell proliferation and in vitro regeneration in Nicotiana benthamiana
Year:
2009
Source of publication :
Plant Science
Authors :
אור, אתי
;
.
דגני, עודד
;
.
סהר, נחמן
;
.
פליישמן, משה
;
.
פרל, אבי
;
.
Volume :
176
Co-Authors:
Hanania, U., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Velcheva, M., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Sahar, N., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Flaishman, M., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Or, E., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Dgani, O., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Perl, A., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Facilitators :
From page:
566
To page:
574
(
Total pages:
9
)
Abstract:
Ubiquitin is a highly conserved 76-amino-acid protein found in all eukaryotic cells. Ubiquitin's expression is encoded and expressed as multimeric head-to-tail repeats (polyubiquitins) that are post-translationally cleaved into monomers, or fused with ribosomal proteins S27a and L40. S27a is highly expressed in meristematic tissues, pollen and ovules and its ubiquitin moiety is thought to act as a chaperone in ribosome biogenesis prior to cleavage. This study suggests that the ribosomal protein S27a plays a critical role in the allocation of meristematic cells that differentiate into lateral structures such as leaves and flowers. S27a was also found to regulate floral meristem development, possibly through the control of cell proliferation as well as cell identity. Overexpression of S27a was correlated with increased proliferation of undifferentiated cells and arrest of morphologically "normal" shoot and leaf development. The ubiquitin moiety did not affect the localization of S27a, but it did affect its protein level: expression of S27a without the ubiquitin moiety caused a severe reduction in S27a protein level. © 2009.
Note:
Related Files :
Eukaryota
N. benthamiana
Nicotiana benthamiana
Nicotiana tabacum
Shoot apical meristem
Tobacco rattle virus
Ubiquitin extension S27a
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.plantsci.2009.01.019
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
30477
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:54
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Scientific Publication
Suppression and overexpression of ubiquitin extension protein S27a affects cell proliferation and in vitro regeneration in Nicotiana benthamiana
176
Hanania, U., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Velcheva, M., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Sahar, N., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Flaishman, M., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Or, E., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Dgani, O., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Perl, A., Department of Fruit Tree Sciences, Institute of Plant Sciences, Agricultural Research Organization, P.O. Box 6, Bet-Dagan, 50250, Israel
Suppression and overexpression of ubiquitin extension protein S27a affects cell proliferation and in vitro regeneration in Nicotiana benthamiana
Ubiquitin is a highly conserved 76-amino-acid protein found in all eukaryotic cells. Ubiquitin's expression is encoded and expressed as multimeric head-to-tail repeats (polyubiquitins) that are post-translationally cleaved into monomers, or fused with ribosomal proteins S27a and L40. S27a is highly expressed in meristematic tissues, pollen and ovules and its ubiquitin moiety is thought to act as a chaperone in ribosome biogenesis prior to cleavage. This study suggests that the ribosomal protein S27a plays a critical role in the allocation of meristematic cells that differentiate into lateral structures such as leaves and flowers. S27a was also found to regulate floral meristem development, possibly through the control of cell proliferation as well as cell identity. Overexpression of S27a was correlated with increased proliferation of undifferentiated cells and arrest of morphologically "normal" shoot and leaf development. The ubiquitin moiety did not affect the localization of S27a, but it did affect its protein level: expression of S27a without the ubiquitin moiety caused a severe reduction in S27a protein level. © 2009.
Scientific Publication
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