Plant Physiology Preview
Published on February 6, 2003; 10.1104/pp.015628
Received October 3, 2002
Returned for revision November 5, 2002
Accepted December 7, 2002
CsAGP1, a Gibberellin-Responsive Gene from Cucumber Hypocotyls, Encodes a Classical Arabinogalactan Protein and Is Involved in Stem Elongation
Me Hea Park , Yoshihito Suzuki *, Makiko Chono , J. Paul Knox , and Isomaro Yamaguchi
Department of Applied Biological Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan (M.H.P., Y.S., I.Y.); National Agricultural Research Organization, National Institute of Crop Science, Department of Wheat and Barley, 2-1-18 Kannondai, Tsukuba 305-8518, Japan (M.C.); and Centre for Plant Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom (J.P.K.)
* Corresponding author; email: ayoshi{at}pgr1.ch.a.u-tokyo.ac.jp.
Fluorescence differential display was used to isolate the gibberellin (GA)-responsive gene, CsAGP1, from cucumber (Cucumis sativus) hypocotyls. A sequence analysis of CsAGP1 indicated that the gene putatively encodes a "classical" arabinogalactan protein (AGP) in cucumber. Transgenic tobacco (Nicotiana tabacum) plants overexpressing CsAGP1 under the control of the cauliflower mosaic virus 35S promoter produced a Y( Glc)3-reactive proteoglycan in addition to AGPs present in wild-type tobacco plants. Immuno-dot blotting of the product, using anti-AGP antibodies, showed that the CsAGP1 protein had the AGP epitopes common to AGP families. The transcription level of CsAGP1 in cucumber hypocotyls increased in response not only to GA but also to indole-3-acetic acid. Although CsAGP1 is expressed in most vegetative tissues of cucumber, including the shoot apices and roots, the GA treatment resulted in an increase in the mRNA level of CsAGP1 only in the upper part of the hypocotyls. Y(Glc)3, which selectively binds AGPs, inhibited the hormone-promoted elongation of cucumber seedling hypocotyls. Transgenic plants ectopically expressing CsAGP1 showed a taller stature and earlier flowering than the wild-type plants. These observations suggest that CsAGP1 is involved in stem elongation.
This article has been cited by other articles:
|
|
|
|
 
H. S. Sardar, J. Yang, and A. M. Showalter
Molecular Interactions of Arabinogalactan Proteins with Cortical Microtubules and F-Actin in Bright Yellow-2 Tobacco Cultured Cells
Plant Physiology,
December 1, 2006;
142(4):
1469 - 1479.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
X.-C. Tang, Y.-Q. He, Y. Wang, and M.-X. Sun
The role of arabinogalactan proteins binding to Yariv reagents in the initiation, cell developmental fate, and maintenance of microspore embryogenesis in Brassica napus L. cv. Topas
J. Exp. Bot.,
August 1, 2006;
57(11):
2639 - 2650.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. J.D. Lee, Y. Sakata, S.-L. Mau, F. Pettolino, A. Bacic, R. S. Quatrano, C. D. Knight, and J. P. Knox
Arabinogalactan Proteins Are Required for Apical Cell Extension in the Moss Physcomitrella patens
PLANT CELL,
November 1, 2005;
17(11):
3051 - 3065.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
W. Sun, J. Xu, J. Yang, M. J. Kieliszewski, and A. M. Showalter
The Lysine-rich Arabinogalactan-protein Subfamily in Arabidopsis: Gene Expression, Glycoprotein Purification and Biochemical Characterization
Plant Cell Physiol.,
June 1, 2005;
46(6):
975 - 984.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K. Mashiguchi, I. Yamaguchi, and Y. Suzuki
Isolation and Identification of Glycosylphosphatidylinositol-Anchored Arabinogalactan Proteins and Novel {beta}-Glucosyl Yariv-Reactive Proteins from Seeds of Rice (Oryza sativa)
Plant Cell Physiol.,
December 15, 2004;
45(12):
1817 - 1829.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
