Acquisition of Myogenic Specificity through Replacement of One Amino Acid of MASH-1 and Introduction of an Additional alpha -Helical Turn

1999 ◽  
Vol 380 (6) ◽  
Author(s):  
C. Dezan ◽  
D. Meierhans ◽  
A.G.E. Künne ◽  
R.K. Allemann
Keyword(s):  
Transcription Factors ◽  
Amino Acid ◽  
Sequence Specificity ◽  
High Affinity ◽  
E Box ◽  
Helical Turn

AbstractThe homologous transcription factors Myf-5, MyoD, myogenin, MRF-4, and MASH-1 bind with high affinity and modest sequence specificity to DNA containing an E-box (CANNTG). This similarity of the

scholarly journals Dual DNA binding specificity of ADD1/SREBP1 controlled by a single amino acid in the basic helix-loop-helix domain.

1995 ◽  
Vol 15 (5) ◽  
pp. 2582-2588 ◽  
Author(s):  
J B Kim ◽  
G D Spotts ◽  
Y D Halvorsen ◽  
H M Shih ◽  
T Ellenberger ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dna Sequence ◽  
Single Amino Acid ◽  
Bhlh Protein ◽  
Sequence Specificity ◽  
Response Element ◽  
Dna Sequence Specificity ◽  
Basic Helix Loop Helix ◽  
Helix Loop Helix ◽  
E Box

Adipocyte determination- and differentiation-dependent factor 1 (ADD1), a member of the basic helix-loop-helix (bHLH) family of transcription factors, has been associated with both adipocyte differentiation and cholesterol homeostasis (in which case it has been termed SREBP1). Using PCR-amplified binding analysis, we demonstrate that ADD1/SREBP1 has dual DNA sequence specificity, binding to both an E-box motif (ATCACGTGA) and a non-E-box sequence previously shown to be important in cholesterol metabolism, sterol regulatory element 1 (SRE-1; ATCACCCCAC). The ADD1/SREBP1 consensus E-box site is similar to a regulatory sequence designated the carbohydrate response element, defined by its ability to regulate transcription in response to carbohydrate in genes involved in fatty acid and triglyceride metabolism in liver and fat. When expressed in fibroblasts, ADD1/SREBP1 activates transcription through both the carbohydrate response E-box element and SRE-1. Substitution of an atypical tyrosine in the basic region of ADD1/SREBP1 to an arginine found in most bHLH protein causes a restriction to only E-box binding. Conversely, substitution of a tyrosine for the equivalent arginine in another bHLH protein, upstream stimulatory factor, allows this factor to acquire a dual binding specificity similar to that of ADD1/SREBP1. Promoter activation by ADD1/SREBP1 through the carbohydrate response element E box is not sensitive to the tyrosine-to-arginine mutation, while activation through SRE-1 is completely suppressed. These data illustrate that ADD1/SREBP1 has dual DNA sequence specificity controlled by a single amino acid residue; this dual specificity may provide a novel mechanism to coordinate different pathways of lipid metabolism.

scholarly journals Arabidopsis heat shock transcription factor HSFA7b positively mediates salt stress tolerance by binding to an E-box-like motif to regulate gene expression

2019 ◽  
Vol 70 (19) ◽  
pp. 5355-5374 ◽  
Author(s):  
Dandan Zang ◽  
Jingxin Wang ◽  
Xin Zhang ◽  
Zhujun Liu ◽  
Yucheng Wang
Keyword(s):  
Gene Expression ◽  
Transcription Factors ◽  
Heat Shock ◽  
Salt Tolerance ◽  
Stress Responses ◽  
Ion Homeostasis ◽  
Cellulose Synthase ◽  
Regulate Gene Expression ◽  
E Box ◽  
Regulate Gene

Abstract Plant heat shock transcription factors (HSFs) are involved in heat and other abiotic stress responses. However, their functions in salt tolerance are little known. In this study, we characterized the function of a HSF from Arabidopsis, AtHSFA7b, in salt tolerance. AtHSFA7b is a nuclear protein with transactivation activity. ChIP-seq combined with an RNA-seq assay indicated that AtHSFA7b preferentially binds to a novel cis-acting element, termed the E-box-like motif, to regulate gene expression; it also binds to the heat shock element motif. Under salt conditions, AtHSFA7b regulates its target genes to mediate serial physiological changes, including maintaining cellular ion homeostasis, reducing water loss rate, decreasing reactive oxygen species accumulation, and adjusting osmotic potential, which ultimately leads to improved salt tolerance. Additionally, most cellulose synthase-like (CSL) and cellulose synthase (CESA) family genes were inhibited by AtHSFA7b; some of them were randomly selected for salt tolerance characterization, and they were mainly found to negatively modulate salt tolerance. By contrast, some transcription factors (TFs) were induced by AtHSFA7b; among them, we randomly identified six TFs that positively regulate salt tolerance. Thus, AtHSFA7b serves as a transactivator that positively mediates salinity tolerance mainly through binding to the E-box-like motif to regulate gene expression.

The vacuolar amino acid transport system is a novel, direct target of GATA transcription factors

2021 ◽  
Vol 85 (3) ◽  
pp. 587-599
Author(s):  
Akane Sato ◽  
Takumi Kimura ◽  
Kana Hondo ◽  
Miyuki Kawano-Kawada ◽  
Takayuki Sekito
Keyword(s):  
Transcription Factors ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Amino Acid Transporters ◽  
Acid Transport ◽  
Amino Acid Transport System ◽  
Gata Transcription Factor ◽  
Gata Transcription Factors ◽  
Acid Status ◽  
Direct Target

ABSTRACT In Saccharomyces cerevisiae, Avt4 exports neutral and basic amino acids from vacuoles. Previous studies have suggested that the GATA transcription factors, Gln3 and Gat1, which are key regulators that adapt cells in response to changes in amino acid status, are involved in the AVT4 transcription. Here, we show that mutations in the putative GATA-binding sites of the AVT4 promoter reduced AVT4 expression. Consistently, a chromatin immunoprecipitation (ChIP) assay revealed that Gat1-Myc13 binds to the AVT4 promoter. Previous microarray results were confirmed that gln3∆gat1∆ cells showed a decrease in expression of AVT1 and AVT7, which also encode vacuolar amino acid transporters. Additionally, ChIP analysis revealed that the AVT6 encoding vacuolar acidic amino acid exporter represents a new direct target of the GATA transcription factor. The broad effect of the GATA transcription factors on the expression of AVT transporters suggests that vacuolar amino acid transport is integrated into cellular amino acid homeostasis.

scholarly journals Multicomponent differentiation-regulated transcription factors in F9 embryonal carcinoma stem cells.

1991 ◽  
Vol 11 (3) ◽  
pp. 1686-1695 ◽  
Author(s):  
M K Shivji ◽  
N B La Thangue
Keyword(s):  
Stem Cells ◽  
Transcription Factors ◽  
Dna Binding ◽  
Embryonal Carcinoma ◽  
Regulatory Sequence ◽  
Dependent Manner ◽  
Sequence Specificity ◽  
Dna Sequence Specificity ◽  
Cell Extracts

Murine F9 embryonal carcinoma (F9 EC) stem cells have an E1a-like transcription activity that is down-regulated as these cells differentiate to parietal endoderm. For the adenovirus E2A promoter, this activity requires at least two sequence-specific transcription factors, one that binds the cyclic AMP-responsive element (CRE) and the other, DRTF1, the DNA-binding activity of which is down-regulated as F9 EC cells differentiate. Here we report the characterization of several binding activities in F9 EC cell extracts, referred to as DRTF 1a, 1b and 1c, that recognize the DRTF1 cis-regulatory sequence (-70 to -50 region). These activities can be chromatographically separated but are not distinguishable by DNA sequence specificity. Activity 1a is a detergent-sensitive complex in which DNA binding is regulated by phosphorylation. In contrast, activities 1b and 1c are unaffected by these treatments but exist as multicomponent protein complexes even before DNA binding. Two sets of DNA-binding polypeptides, p50DR and p30DR, affinity purified from F9 EC cell extracts produce complexes 1b and 1c. Both polypeptides appear to be present in the same DNA-bound protein complex and both directly contact DNA. These affinity-purified polypeptides activate transcription in vitro in a binding-site-dependent manner. These data indicate the in F9 EC stem cells, multicomponent differentiation-regulated transcription factors contribute to the cellular E1a-like activity.

scholarly journals Distal substitutions drive divergent DNA specificity among paralogous transcription factors through subdivision of conformational space

2015 ◽  
Vol 113 (2) ◽  
pp. 326-331 ◽  
Author(s):  
William H. Hudson ◽  
Bradley R. Kossmann ◽  
Ian Mitchelle S. de Vera ◽  
Shih-Wei Chuo ◽  
Emily R. Weikum ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Amino Acid ◽  
Dna Binding ◽  
Glucocorticoid Receptor ◽  
Binding Specificity ◽  
Conformational Space ◽  
Amino Acid Substitutions ◽  
Ancestral Gene ◽  
Response Elements ◽  
Binding Interface

Many genomes contain families of paralogs—proteins with divergent function that evolved from a common ancestral gene after a duplication event. To understand how paralogous transcription factors evolve divergent DNA specificities, we examined how the glucocorticoid receptor and its paralogs evolved to bind activating response elements [(+)GREs] and negative glucocorticoid response elements (nGREs). We show that binding to nGREs is a property of the glucocorticoid receptor (GR) DNA-binding domain (DBD) not shared by other members of the steroid receptor family. Using phylogenetic, structural, biochemical, and molecular dynamics techniques, we show that the ancestral DBD from which GR and its paralogs evolved was capable of binding both nGRE and (+)GRE sequences because of the ancestral DBD’s ability to assume multiple DNA-bound conformations. Subsequent amino acid substitutions in duplicated daughter genes selectively restricted protein conformational space, causing this dual DNA-binding specificity to be selectively enhanced in the GR lineage and lost in all others. Key substitutions that determined the receptors’ response element-binding specificity were far from the proteins’ DNA-binding interface and interacted epistatically to change the DBD’s function through DNA-induced allosteric mechanisms. These amino acid substitutions subdivided both the conformational and functional space of the ancestral DBD among the present-day receptors, allowing a paralogous family of transcription factors to control disparate transcriptional programs despite high sequence identity.

The SLC1 high-affinity glutamate and neutral amino acid transporter family

2013 ◽  
Vol 34 (2-3) ◽  
pp. 108-120 ◽  
Author(s):  
Yoshikatsu Kanai ◽  
Benjamin Clémençon ◽  
Alexandre Simonin ◽  
Michele Leuenberger ◽  
Martin Lochner ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Transporter ◽  
Neutral Amino Acid ◽  
High Affinity ◽  
Neutral Amino Acid Transporter ◽  
Transporter Family ◽  
Acid Transporter

scholarly journals Interacting Transcription Factors from the Three-Amino Acid Loop Extension Superclass Regulate Tuber Formation

2003 ◽  
Vol 132 (3) ◽  
pp. 1391-1404 ◽  
Author(s):  
Hao Chen ◽  
Faye M. Rosin ◽  
Salomé Prat ◽  
David J. Hannapel
Keyword(s):  
Transcription Factors ◽  
Amino Acid ◽  
Tuber Formation

Single amino acid changes which alter the sequence specificity of the T4 and T2 (Dam) DNA-adenine methyltransferases

Gene ◽  
1988 ◽  
Vol 74 (1) ◽  
pp. 275-276 ◽  
Author(s):  
Zoe Miner ◽  
Samuel Schlagman ◽  
Stanley Hattman
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Sequence Specificity
Sign in / Sign up

Export Citation Format

Share Document