GTC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Okanami, M
Right arrow Articles by Iwabuchi, M
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Okanami, M
Right arrow Articles by Iwabuchi, M
GENES CELLS (1996) 1, 87-99.
Copyright © 1996 Blackwell Publishing or its licensors

Original Article

HALF-1, a bZIP-type protein, interacting with the wheat transcription factor HBP-1a contains a novel transcriptional activation domain

M Okanami, T Meshi, H Tamai, and M Iwabuchi

BACKGROUND: Nuclear factors bind to cis-acting elements and mediate transcriptional regulation through protein-protein interactions with other factors. The bZIP-type wheat nuclear protein HBP-1a(17) is a putative transcriptional activator specifically binding to the Hex (ccACGTCA) and G-box (CCACGTGG) motifs, which are often found in the cis-acting elements critical for various responses in plants. RESULTS: In order to investigate the mechanisms for gene expression mediated via the Hex and G-box motifs, we attempted to isolate proteins interacting with HBP-1a(17) based on protein-protein interactions. A cDNA expression library from wheat seedlings was screened with 32P-labelled HBP-1a(17), and a bZIP-type protein, termed HALF-1 (HBP-1-associated leucine-zipper factor-1), was isolated. GST-pulldown assay, yeast two-hybrid system and EMSA showed that HALF-1 and HBP-1a(17) interact with each other through their leucine-zipper regions. Dissection experiments showed that HALF-1 has at least one potential trans-activation domain which includes a nine amino acid motif conserved between several plant bZIP-type proteins. This motif, named GCB (GBF-conserved box; consensus, NLNIGMDXW), activated the expression of a reporter gene, when fused to the GAL4 DNA-binding domain. The corresponding region of Arabidopsis GBF1 also stimulated transcription. However, the trans-activation domain of HALF-1 did not function in yeast. CONCLUSIONS: We identified a novel trans-activation domain which contains the GCB motif conserved among plant bZIP-type factors. The trans-activation appears to be mediated by interaction between the GCB motif and a factor conserved in plants.


This article has been cited by other articles:


Home page
 Plant Physiol.Home page
A. Nijhawan, M. Jain, A. K. Tyagi, and J. P. Khurana
Genomic Survey and Gene Expression Analysis of the Basic Leucine Zipper Transcription Factor Family in Rice
Plant Physiology, February 1, 2008; 146(2): 333 - 350.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
H. Tamai, M. Iwabuchi, and T. Meshi
Arabidopsis GARP Transcriptional Activators Interact with the Pro-Rich Activation Domain Shared by G-Box-Binding bZIP Factors
Plant Cell Physiol., January 1, 2002; 43(1): 99 - 107.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
T. Hobo, Y. Kowyama, and T. Hattori
A bZIP factor, TRAB1, interacts with VP1 and mediates abscisic acid-induced transcription
PNAS, December 21, 1999; 96(26): 15348 - 15353.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS
Copyright © 1996 by Wiley-Blackwell Publishing.