scholarly journals VP16 fusion efficiently reveals the function of transcriptional repressors in Arabidopsis

2014 ◽  
Vol 31 (2) ◽  
pp. 123-132 ◽  
Author(s):  
Sumire Fujiwara ◽  
Keiko Kigoshi ◽  
Nobutaka Mitsuda ◽  
Kaoru Suzuki ◽  
Masaru Ohme-Takagi
FEBS Letters ◽  
2014 ◽  
Vol 588 (20) ◽  
pp. 3665-3672 ◽  
Author(s):  
Sumire Fujiwara ◽  
Shingo Sakamoto ◽  
Keiko Kigoshi ◽  
Kaoru Suzuki ◽  
Masaru Ohme-Takagi

2017 ◽  
Author(s):  
TL Vu-Han ◽  
S Buhs ◽  
H Gerull ◽  
M Horstmann ◽  
P Nollau

Nature ◽  
2020 ◽  
Author(s):  
Jekaterina Truskina ◽  
Jingyi Han ◽  
Elina Chrysanthou ◽  
Carlos S. Galvan-Ampudia ◽  
Stéphanie Lainé ◽  
...  

2003 ◽  
Vol 185 (24) ◽  
pp. 7145-7152 ◽  
Author(s):  
E.-H. Lee ◽  
C. Rouquette-Loughlin ◽  
J. P. Folster ◽  
W. M. Shafer

ABSTRACT The farAB operon of Neisseria gonorrhoeae encodes an efflux pump which mediates gonococcal resistance to antibacterial fatty acids. It was previously observed that expression of the farAB operon was positively regulated by MtrR, which is a repressor of the mtrCDE-encoded efflux pump system (E.-H. Lee and W. M. Shafer, Mol. Microbiol. 33:839-845, 1999). This regulation was believed to be indirect since MtrR did not bind to the farAB promoter. In this study, computer analysis of the gonococcal genome sequence database, lacZ reporter fusions, and gel mobility shift assays were used to elucidate the regulatory mechanism by which expression of the farAB operon is modulated by MtrR in gonococci. We identified a regulatory protein belonging to the MarR family of transcriptional repressors and found that it negatively controls expression of farAB by directly binding to the farAB promoter. We designated this regulator FarR to signify its role in regulating the farAB operon. We found that MtrR binds to the farR promoter, thereby repressing farR expression. Hence, MtrR regulates farAB in a positive fashion by modulating farR expression. This MtrR regulatory cascade seems to play an important role in adjusting levels of the FarAB and MtrCDE efflux pumps to prevent their excess expression in gonococci.


2007 ◽  
Vol 86 (6) ◽  
pp. 393-401 ◽  
Author(s):  
Raz Somech ◽  
Einav Nili Gal-Yam ◽  
Sigal Shaklai ◽  
Orit Geller ◽  
Ninette Amariglio ◽  
...  

Development ◽  
1997 ◽  
Vol 124 (20) ◽  
pp. 4133-4141 ◽  
Author(s):  
H. Kato ◽  
Y. Taniguchi ◽  
H. Kurooka ◽  
S. Minoguchi ◽  
T. Sakai ◽  
...  

Notch is involved in the cell fate determination of many cell lineages. The intracellular region (RAMIC) of Notch1 transactivates genes by interaction with a DNA binding protein RBP-J. We have compared the activities of mouse RAMIC and its derivatives in transactivation and differentiation suppression of myogenic precursor cells. RAMIC comprises two separate domains, IC for transactivation and RAM for RBP-J binding. Although the physical interaction of IC with RBP-J was much weaker than with RAM, transactivation activity of IC was shown to involve RBP-J by using an RBP-J null mutant cell line. IC showed differentiation suppression activity that was generally comparable to its transactivation activity. The RBP-J-VP16 fusion protein, which has strong transactivation activity, also suppressed myogenesis of C2C12. The RAM domain, which has no other activities than binding to RBP-J, synergistically stimulated transactivation activity of IC to the level of RAMIC. The RAM domain was proposed to compete with a putative co-repressor for binding to RBP-J because the RAM domain can also stimulate the activity of RBP-J-VP16. These results taken together, indicate that differentiation suppression of myogenic precursor cells by Notch signalling is due to transactivation of genes carrying RBP-J binding motifs.


Metallomics ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 1476-1500 ◽  
Author(s):  
Rima Roy ◽  
Saikat Samanta ◽  
Surajit Patra ◽  
Nav Kumar Mahato ◽  
Rudra P. Saha

The ArsR-SmtB family of transcriptional repressors regulates the transcription of metal-efflux proteins by binding specific metals at a variety of secondary structural elements, called motifs, on the surface of the proteins.


2005 ◽  
Vol 386 (2) ◽  
pp. 95-99 ◽  
Author(s):  
Alexander E.F. Smith ◽  
Farzin Farzaneh ◽  
Kevin G. Ford

AbstractIn order to demonstrate that an existing zinc-finger protein can be simply modified to enhance DNA binding and sequence discrimination in both episomal and chromatin contexts using existing zinc-finger DNA recognition code data, and without recourse to phage display and selection strategies, we have examined the consequences of a single zinc-finger extension to a synthetic three-zinc-finger VP16 fusion protein, on transcriptional activation from model target promoters harbouring the zinc-finger binding sequences. We report a nearly 10-fold enhanced transcriptional activation by the four-zinc-finger VP16 fusion protein relative to the progenitor three-finger VP16 protein in transient assays and a greater than five-fold enhancement in stable reporter-gene expression assays. A marked decrease in transcriptional activation was evident for the four-zinc-finger derivative from mutated regulatory regions compared to the progenitor protein, as a result of recognition site-size extension. This discriminatory effect was shown to be protein concentration-dependent. These observations suggest that four-zinc-finger proteins are stable functional motifs that can be a significant improvement over the progenitor three-zinc-finger protein, both in terms of specificity and the ability to target transcriptional function to promoters, and that single zinc-finger extension can therefore have a significant impact on DNA zinc-finger protein interactions. This is a simple route for modifying or enhancing the binding properties of existing synthetic zinc-finger-based transcription factors and may be particularly suited for the modification of endogenous zinc-finger transcription factors for promoter biasing applications.


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