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Genome-wide DNA binding of GBF1 is modulated by its heterodimerizing protein partners, HY5 and HYH

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Title Genome-wide DNA binding of GBF1 is modulated by its heterodimerizing protein partners, HY5 and HYH
 
Creator Ram, Hathi
Priya, Pushp
Jain, Mukesh
Chattopadhyay, Sudip
 
Description Accepted date: 7 October 2013
In today’s post-genomic era where direct targets of many
transcription factors have been identified, it is becoming
increasingly evident that transcriptional networks are very
complex. Heterodimerization of transcription factors is one
of the several methods by which these complex transcriptional networks are formed. By heterodimerization, DNA-
binding specificity and affinity, transactivation properties,
and ultimately cell physiology might be altered (Naar et al.,
2001). The formation of heterodimers has the potential to
recognize additional binding sites and increase the range
of DNA-binding specificity (Foster et al., 1994). Further, heterodimerization also allows the production of new protein
configurations. For example, the protein STF1 from soybean
can dimerize with GBF proteins and this dimerization brings
together the acidic region from STF1 and the proline-rich
region of the GBF proteins into one binding element (Cheong
et al., 1998). These results highlight the importance and/or
consequences of heterodimerization of transcription factors
at particular locus. However, to understand the complex transcriptional networks, it is important to investigate that how
heterodimerization affects the whole-genome-wide binding and transcriptional properties of a transcription factor.
Here in this study, we have investigated genome-wide DNA
binding of bZIP transcription factor GBF1, and analyzed the
importance of its heterodimerization with HY5 and HYH for
its genome-wide binding. We have found that GBF1 binding
sites are enriched within the 1-kb regions upstream to the
transcription start sites of target genes. Moreover, the bindings of GBF1 to most of its targets are largely dependent on
HY5, while HYH only affects the binding of GBF1 to some
specific sites.
This work is supported by the J.C. Bose National Fellowship
Grant of Department of Science and Technology, Government
of India to S.C.; and the core grant of the National Institute
for Plant Genome Research to M.J. H.R. and P.P. are recipients
of CSIR fellowships, Government of India. No conflict of interest declared.
 
Date 2015-12-22T06:59:05Z
2015-12-22T06:59:05Z
2014
 
Type Article
 
Identifier Mol. Plant, 7(2): 448-451
1752-9867
http://172.16.0.77:8080/jspui/handle/123456789/443
http://www.sciencedirect.com/science/article/pii/S1674205214603026
10.1093/mp/sst143
 
Language en_US
 
Publisher Elsevier B.V.