The Arabidopsis homolog of trithorax, ATX1, binds phosphatidylinositol 5-phosphate, and the two regulate a common set of target genes

被引：113
作者：
Alvarez-Venegas, R
Sadder, M
Hlavacka, A
Baluska, F
Xia, YN
Lu, GQ
Firsov, A
Sarath, G
Moriyama, H
Dubrovsky, JG
Avramova, Z [1 ]
机构：
[1] Univ Nebraska, Sch Biol Sci, Lincoln, NE 68588 USA
[2] Univ Bonn, Inst Bot, Dept Plant Cell Biol, D-53115 Bonn, Germany
[3] Univ Nebraska, Ctr Biotechnol, Genom Core Res Facil, Lincoln, NE 68588 USA
[4] Univ Nebraska, Ctr Biotechnol, Bioinformat Core Res Facil, Lincoln, NE 68588 USA
[5] Univ Nebraska, USDA, Agr Res Serv Unit, Lincoln, NE 68583 USA
[6] Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA
[7] Univ Nacl Autonoma Mexico, Inst Biotecnol, Cuernavaca 62250, Morelos, Mexico
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2006年 / 103卷 / 15期
关键词：
epigenetic regulation; lipid signaling;
D O I：
10.1073/pnas.0600944103
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The Arabidopsis homolog of trithorax, ATX1, regulates numerous functions in Arabidopsis beyond the homeotic genes. Here, we identified genome-wide targets of ATX1 and showed that ATX1 is a receptor for a lipid messenger, phosphatidylinositol 5-phosphate, PI5P. PI5P negatively affects ATX1 activity, suggesting a regulatory pathway connecting lipid-signaling with nuclear functions. We propose a model to illustrate how plants may respond to stimuli (external or internal) that elevate cellular PI5P levels by altering expression of ATX1-controlled genes.
引用
收藏
页码：6049 / 6054
页数：6
相关论文
共 36 条
[11]   The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor [J].
Gozani, O ;
Karuman, P ;
Jones, DR ;
Ivanov, D ;
Cha, J ;
Lugovskoy, AA ;
Baird, CL ;
Zhu, H ;
Field, SJ ;
Lessnick, SL ;
Villasenor, J ;
Mehrotra, B ;
Chen, J ;
Rao, VR ;
Brugge, JS ;
Ferguson, CG ;
Payrastre, B ;
Myszka, DG ;
Cantley, LC ;
Wagner, G ;
Divecha, N ;
Prestwich, GD ;
Yuan, JY .
CELL, 2003, 114 (01) :99-111
[12]   The MYST domain acetyltransferase Chameau functions in epigenetic mechanisms of transcriptional repression [J].
Grienenberger, A ;
Miotto, B ;
Sagnier, T ;
Cavalli, G ;
Schramke, V ;
Geli, V ;
Mariol, MC ;
Berenger, H ;
Graba, Y ;
Pradel, J .
CURRENT BIOLOGY, 2002, 12 (09) :762-766
[13]  
GUI X, 1998, NAT GENET, V18, P331
[14]   Linking lipids to chromatin [J].
Jones, DR ;
Divecha, N .
CURRENT OPINION IN GENETICS & DEVELOPMENT, 2004, 14 (02) :196-202
[15]   Structural mechanism of endosome docking by the FYVE domain [J].
Kutateladze, T ;
Overduin, M .
SCIENCE, 2001, 291 (5509) :1793-1796
[16]   Biochemical analyses of the AF10 protein: The extended LAP/PHD-finger mediates oligomerisation [J].
Linder, B ;
Newman, R ;
Jones, LK ;
Debernardi, S ;
Young, BD ;
Freemont, P ;
Verrijzer, CP ;
Saha, V .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 299 (02) :369-378
[17]   THE TRITHORAX GENE, A TRANS-ACTING REGULATOR OF THE BITHORAX COMPLEX IN DROSOPHILA, ENCODES A PROTEIN WITH ZINC-BINDING DOMAINS [J].
MAZO, AM ;
HUANG, DH ;
MOZER, BA ;
DAWID, IB .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (06) :2112-2116
[18]   Identification of a new polyphosphoinositide in plants, phosphatidylinositol 5-monophosphate (PtIns5P), and its accumulation upon osmotic stress [J].
Meijer, HJG ;
Berrie, CP ;
Iurisci, C ;
Divecha, N ;
Musgrave, A ;
Munnik, T .
BIOCHEMICAL JOURNAL, 2001, 360 :491-498
[19]   MLL targets SET domain methyltransferase activity to Hox gene promoters [J].
Milne, TA ;
Briggs, SD ;
Brock, HW ;
Martin, ME ;
Gibbs, D ;
Allis, CD ;
Hess, JL .
MOLECULAR CELL, 2002, 10 (05) :1107-1117
[20]   Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9 [J].
Mochizuki, Y ;
Majerus, PW .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (17) :9768-9773
1234