PMID- 21834856
OWN - NLM
STAT- MEDLINE
DCOM- 20120301
LR  - 20220321
IS  - 1399-3054 (Electronic)
IS  - 0031-9317 (Linking)
VI  - 143
IP  - 3
DP  - 2011 Nov
TI  - The purine-rich DNA-binding protein OsPuralpha participates in the regulation of the 
      rice sucrose synthase 1 gene expression.
PG  - 219-34
LID - 10.1111/j.1399-3054.2011.01501.x [doi]
AB  - The rice sucrose synthase 1 (RSus1) gene is transcriptionally induced by sucrose, 
      and a region within its promoter, at -1117 to -958 upstream of the transcription 
      initiation site, was found to be essential for enhancing the sucrose-induced 
      expression. Further dissection of this region revealed that a group of nuclear 
      proteins interact with a 39-bp fragment named A-3-2 (-1045 to -1007). A protein 
      that specifically and directly interacted with A-3-2 was isolated from the 
      suspension-cultured cells of rice and was subsequently identified as a 
      purine-rich DNA-binding protein. The amino acid sequence of this protein, OsPuralpha, 
      exhibited 73% identity with the Arabidopsis Puralpha-1 protein, and its modeled 
      structure resembled the structure of Pur-alpha in Drosophila. Recombinant OsPuralpha 
      expressed and purified from Escherichia coli was demonstrated to have DNA-binding 
      activity and to interact with A-3-2 specifically. Moreover, OsPuralpha was able to 
      enhance sucrose-induced expression of the beta-glucuronidase (GUS) reporter gene, 
      which was transcriptionally fused to two copies of a DNA fragment containing 
      A-3-2 and the cauliflower mosaic virus 35S minimal promoter, in vivo. The level 
      of OsPuralpha bound to A-3-2 was higher in cells cultured in the presence of sucrose; 
      however, the level of OsPuralpha mRNA in cells was not affected by sucrose. The 
      results of this study demonstrate that OsPuralpha participates in the regulation of 
      RSus1 expression in response to sucrose; nevertheless, it may require other 
      partner proteins for full function.
CI  - Copyright (c) Physiologia Plantarum 2011.
FAU - Chang, Jui-Che
AU  - Chang JC
AD  - Department of Biochemical Science and Technology, National Taiwan University, 
      Taipei, Taiwan.
FAU - Liao, Yi-Chun
AU  - Liao YC
FAU - Yang, Chien-Chih
AU  - Yang CC
FAU - Wang, Ai-Yu
AU  - Wang AY
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110920
PL  - Denmark
TA  - Physiol Plant
JT  - Physiologia plantarum
JID - 1256322
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Plant Proteins)
RN  - 135687-69-3 (Osgrp1 protein, Oryza sativa)
RN  - 57-50-1 (Sucrose)
RN  - EC 2.4.1.- (Glucosyltransferases)
RN  - EC 2.4.1.13 (sucrose synthase)
RN  - EC 3.2.1.31 (Glucuronidase)
SB  - IM
MH  - DNA-Binding Proteins/*genetics/metabolism
MH  - *Gene Expression Regulation, Plant
MH  - Genes, Reporter
MH  - Glucosyltransferases/biosynthesis/*genetics
MH  - Glucuronidase/biosynthesis/genetics
MH  - Molecular Sequence Data
MH  - Molecular Structure
MH  - Oryza/enzymology/*genetics/metabolism
MH  - Plant Proteins/*metabolism
MH  - Plants, Genetically Modified/genetics/metabolism
MH  - Sequence Analysis, Protein
MH  - Sucrose/metabolism
EDAT- 2011/08/13 06:00
MHDA- 2012/03/02 06:00
CRDT- 2011/08/13 06:00
PHST- 2011/08/13 06:00 [entrez]
PHST- 2011/08/13 06:00 [pubmed]
PHST- 2012/03/02 06:00 [medline]
AID - 10.1111/j.1399-3054.2011.01501.x [doi]
PST - ppublish
SO  - Physiol Plant. 2011 Nov;143(3):219-34. doi: 10.1111/j.1399-3054.2011.01501.x. 
      Epub 2011 Sep 20.