scholarly journals Nuclear protein 1 induced by ATF4 in response to various stressors acts as a positive regulator on the transcriptional activation of ATF4

IUBMB Life ◽  
2009 ◽  
Vol 61 (12) ◽  
pp. 1153-1158 ◽  
Author(s):  
Hyeon-Ok Jin ◽  
Sung-Keum Seo ◽  
Sang-Hyeok Woo ◽  
Tae-Boo Choe ◽  
Seok-Il Hong ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Nuclear Protein ◽  
Positive Regulator

bFGF induces BCK promoter-driven expression in muscle via increased binding of a nuclear protein

1997 ◽  
Vol 273 (1) ◽  
pp. C223-C229 ◽  
Author(s):  
L. Kim ◽  
A. Steves ◽  
M. Collins ◽  
J. Fu ◽  
M. E. Ritchie
Keyword(s):  
Transcription Factor ◽  
Creatine Kinase ◽  
Transcriptional Activation ◽  
Culture Medium ◽  
Nuclear Protein ◽  
C2c12 Cells ◽  
Nuclear Factor ◽  
Muscle Creatine Kinase ◽  
Responsive Element ◽  
Brain Creatine Kinase

Changes in gene expression occurring during skeletal muscle differentiation are exemplified by downregulation of brain creatine kinase (BCK) and induction of muscle creatine kinase (MCK). Although both are transcriptionally regulated, there appears to be no transcription factor-element overlap, suggesting that their coordinate expression results from culture medium-related influences. Basic fibroblast growth factor (bFGF) prevents myogenesis and represses MCK expression by inhibiting transcriptional activation. It was hypothesized that bFGF similarly influenced BCK by inducing its expression. Accordingly, BCK promoter constructs were transiently transfected into C2C12 cells and, after a switch to differentiation medium, were treated with bFGF, bFGF plus herbimycin, adenosine 3',5'-cyclic monophosphate (cAMP), or phorbol 12-myristate 13-acetate (PMA). Analyses demonstrated that bFGF responsiveness was contained within a 33-base pair element. Electromobility shift assays showed that bFGF induction increased the abundance of the nuclear factor binding the element. Both effects were prevented by herbimycin. Neither cAMP nor PMA specifically induced the construct containing the bFGF-responsive element. The induced factor required phosphorylation to bind, implying that bFGF-mediated increases in binding may be due to transcription factor phosphorylation.

scholarly journals The Transcriptional Co-activator p/CIP (NCoA-3) Is Up-regulated by STAT6 and Serves as a Positive Regulator of Transcriptional Activation by STAT6

2004 ◽  
Vol 279 (30) ◽  
pp. 31105-31112 ◽  
Author(s):  
Akinori Arimura ◽  
Maartje van Peer ◽  
Andreas J. Schröder ◽  
Paul B. Rothman
Keyword(s):  
Transcriptional Activation ◽  
Positive Regulator

scholarly journals MCMBP maintains genome integrity by protecting the MCM subunits from degradation

2019 ◽  
Author(s):  
Venny Santosa ◽  
Masato T. Kanemaki
Keyword(s):  
Dna Damage ◽  
Dna Replication ◽  
Transcriptional Activation ◽  
Damage Accumulation ◽  
Nuclear Protein ◽  
De Novo ◽  
Genome Integrity ◽  
De Novo Synthesis ◽  
Eukaryotic Dna ◽  
High Level

AbstractThe hetero-hexameric MCM2–7 helicase plays a central role in eukaryotic DNA replication. The expression of MCM2–7 is maintained at a high level for creating dormant origins, which are important for maintaining genome integrity. However, other than transcriptional activation for the de novo synthesis, little is known about how cells maintain a high level of MCM2–7. We show that human MCMBP is a short-lived nuclear protein associating mainly with MCM5, 6, and 7. Loss of MCMBP down-regulates MCM2–7, leading to replication stress and DNA-damage accumulation. Our work demonstrates MCMBP protects the MCM subunits from degradation and suggests its chaperone-like role to achieve a high level of functional MCM2–7 using the nascent and recycled subunits.

scholarly journals Binding site requirements for pea nuclear protein factor GT-1 correlate with sequences required for light-dependent transcriptional activation of the rbcS-3A gene.

1988 ◽  
Vol 7 (13) ◽  
pp. 4035-4044 ◽  
Author(s):  
P. J. Green ◽  
M. H. Yong ◽  
M. Cuozzo ◽  
Y. Kano-Murakami ◽  
P. Silverstein ◽  
...  
Keyword(s):  
Binding Site ◽  
Transcriptional Activation ◽  
Nuclear Protein ◽  
Protein Factor

scholarly journals NRC-Interacting Factor 1 Is a Novel Cotransducer That Interacts with and Regulates the Activity of the Nuclear Hormone Receptor Coactivator NRC

2002 ◽  
Vol 22 (19) ◽  
pp. 6883-6894 ◽  
Author(s):  
Muktar A. Mahajan ◽  
Audrey Murray ◽  
Herbert H. Samuels
Keyword(s):  
Amino Acid ◽  
Transcriptional Activation ◽  
Transcriptional Activity ◽  
Hormone Receptors ◽  
Nuclear Protein ◽  
Zinc Fingers ◽  
Nuclear Hormone Receptor ◽  
Coactivator Complex

ABSTRACT We previously reported the cloning and characterization of a novel nuclear hormone receptor transcriptional coactivator, which we refer to as NRC. NRC is a 2,063-amino-acid nuclear protein which contains a potent N-terminal activation domain and several C-terminal modules which interact with CBP and ligand-bound nuclear hormone receptors as well as c-Fos and c-Jun. In this study we sought to clone and identify novel factors that interact with NRC to modulate its transcriptional activity. Here we describe the cloning and characterization of a novel protein we refer to as NIF-1 (NRC-interacting factor 1). NIF-1 was cloned from rat pituitary and human cell lines and was found to interact in vivo and in vitro with NRC. NIF-1 is a 1,342-amino-acid nuclear protein containing a number of conserved domains, including six Cys-2/His-2 zinc fingers, an N-terminal stretch of acidic amino acids, and a C-terminal leucine zipper-like motif. Zinc fingers 1 to 3 are potential DNA-binding BED finger domains recently proposed to play a role in altering local chromatin architecture. We mapped the interaction domains of NRC and NIF-1. Although NIF-1 does not directly interact with nuclear receptors, it markedly enhances ligand-dependent transcriptional activation by nuclear hormone receptors in vivo as well as activation by c-Fos and c-Jun. These results, and the finding that NIF-1 interacts with NRC in vivo, suggest that NIF-1 functions to regulate transcriptional activation through NRC. We suggest that NIF-1, and factors which associate with coactivators but not receptors, be referred to as cotransducers, which act in vivo either as part of a coactivator complex or downstream of a coactivator complex to modulate transcriptional activity. Our findings suggest that NIF-1 may be a functional component of an NRC complex and acts as a regulator or cotransducer of NRC function.

scholarly journals CaWRKY28 Cys249 is required for interaction with CaWRKY40 in the regulation of pepper immunity to Ralstonia solanacearum

2021 ◽  
Author(s):  
Sheng Yang ◽  
Yangwen Zhang ◽  
Weiwei Cai ◽  
Cailing Liu ◽  
Jiong Hu ◽  
...  
Keyword(s):  
Ralstonia Solanacearum ◽  
Target Gene ◽  
Target Genes ◽  
Nuclear Protein ◽  
Bimolecular Fluorescence Complementation ◽  
Physical Interaction ◽  
Wrky Transcription Factors ◽  
Related Target ◽  
Microscale Thermophoresis ◽  
Positive Regulator

WRKY transcription factors have been implicated in plant response to pathogens, but how WRKY-mediated networks are organized and operate to produce appropriate transcriptional outputs remains largely unclear. Here, we identify a member of the WRKY family from pepper (Capsicum annuum), CaWRKY28, that physically interacts with CaWRKY40, a positive regulator of pepper immunity and thermotolerance. We confirmed CaWRKY28/CaWRKY40 interaction by co-immunoprecipitation, bimolecular fluorescence complementation and microscale thermophoresis. Our findings supported that CaWRKY28 is a nuclear protein that acts as positive regulator in pepper responses to the pathogenic bacterium Ralstonia solanacearum infection. It performs its function not by directly modulating the W-box containing immunity related genes but by promoting CaWRKY40 via physical interaction to bind and activate its immunity related target genes including CaPR1, CaNPR1, CaDEF1 and CaABR1, but not its thermotolerance related target gene CaHSP24. All these data indicate that CaWRKY28 interacts with and potentiates CaWRKY40 in regulating immunity against R. solanacearum infection but not thermotolerance. Importantly, we discovered that CaWRKY28 Cys249, shared by CaWRKY28 and its orthologs probably only in the Solanaceae, is crucial for the CaWRKY28-CaWRKY40 interaction. These results highlight how CaWRKY28 associates with CaWRKY40 during the establishment of WRKY networks, and how CaWRKY40 achieves its functional specificity during pepper responses to R. solanacearum infection.

ABT1-associated protein (ABTAP), a novel nuclear protein conserved from yeast to mammals, represses transcriptional activation by ABT1

2004 ◽  
Vol 93 (4) ◽  
pp. 788-806 ◽  
Author(s):  
Tsukasa Oda ◽  
Aya Fukuda ◽  
Hiroko Hagiwara ◽  
Yasuhiko Masuho ◽  
Masa-aki Muramatsu ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Nuclear Protein
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