A plant leucine zipper protein that recognizes an abscisic acid response element

Science ◽  
1990 ◽  
Vol 250 (4978) ◽  
pp. 267-271 ◽  
Author(s):  
M. Guiltinan ◽  
W. Marcotte ◽  
R. Quatrano
Keyword(s):  
Abscisic Acid ◽  
Leucine Zipper ◽  
Response Element ◽  
Leucine Zipper Protein

A Plant Leucine Zipper Protein That Recognizes an Abscisic Acid Response Element

Science ◽  
1990 ◽  
Vol 250 (4981) ◽  
pp. 612-612 ◽  
Author(s):  
M. J. Guiltinan ◽  
W. R. Marcotte ◽  
R. S. Quatrano
Keyword(s):  
Abscisic Acid ◽  
Leucine Zipper ◽  
Response Element ◽  
Leucine Zipper Protein

scholarly journals Abscisic acid signaling is controlled by a BRANCHED1/HD-ZIP I cascade in Arabidopsis axillary buds

2016 ◽  
Vol 114 (2) ◽  
pp. E245-E254 ◽  
Author(s):  
Eduardo González-Grandío ◽  
Alice Pajoro ◽  
José M. Franco-Zorrilla ◽  
Carlos Tarancón ◽  
Richard G. H. Immink ◽  
...  
Keyword(s):  
Abscisic Acid ◽  
Leucine Zipper ◽  
Crop Breeding ◽  
Branching Patterns ◽  
Genetic Module ◽  
Homeobox Protein ◽  
Branch Development ◽  
Key Aspects ◽  
Encoding Genes ◽  
Leucine Zipper Protein

Shoot-branching patterns determine key aspects of plant life and are important targets for crop breeding. However, we are still largely ignorant of the genetic networks controlling locally the most important decision during branch development: whether the axillary bud, or branch primordium, grows out to give a lateral shoot or remains dormant. Here we show that, inside the buds, the TEOSINTE BRANCHED1, CYCLOIDEA, PCF (TCP) transcription factor BRANCHED1 (BRC1) binds to and positively regulates the transcription of three related Homeodomain leucine zipper protein (HD-ZIP)-encoding genes: HOMEOBOX PROTEIN 21 (HB21), HOMEOBOX PROTEIN 40 (HB40), and HOMEOBOX PROTEIN 53 (HB53). These three genes, together with BRC1, enhance 9-CIS-EPOXICAROTENOID DIOXIGENASE 3 (NCED3) expression, lead to abscisic acid accumulation, and trigger hormone response, thus causing suppression of bud development. This TCP/HD-ZIP genetic module seems to be conserved in dicot and monocotyledonous species to prevent branching under light-limiting conditions.

scholarly journals IFP 35 is an interferon-induced leucine zipper protein that undergoes interferon-regulated cellular redistribution.

1994 ◽  
Vol 269 (2) ◽  
pp. 1091-1098
Author(s):  
F.C. Bange ◽  
U. Vogel ◽  
T. Flohr ◽  
M. Kiekenbeck ◽  
B. Denecke ◽  
...  
Keyword(s):  
Leucine Zipper ◽  
Leucine Zipper Protein

scholarly journals Role of small leucine zipper protein in hepatic gluconeogenesis and metabolic disorder

2020 ◽  
Author(s):  
Minsoo Kang ◽  
Sun Kyoung Han ◽  
Suhyun Kim ◽  
Sungyeon Park ◽  
Yerin Jo ◽  
...  
Keyword(s):  
Blood Glucose ◽  
Glucose Metabolism ◽  
Metabolic Disorder ◽  
Leucine Zipper ◽  
Metabolic Diseases ◽  
Adenosine Monophosphate ◽  
The Body ◽  
Hepatic Gluconeogenesis ◽  
Leucine Zipper Protein

Abstract Hepatic gluconeogenesis is the central pathway for glucose generation in the body. The imbalance between glucose synthesis and uptake leads to metabolic diseases such as obesity, diabetes, and cardiovascular diseases. Small leucine zipper protein (sLZIP) is an isoform of LZIP and it mainly functions as a transcription factor. Although sLZIP is known to regulate the transcription of genes involved in various cellular processes, the role of sLZIP in hepatic glucose metabolism is not known. In this study, we investigated the regulatory role of sLZIP in hepatic gluconeogenesis and its involvement in metabolic disorder. We found that sLZIP expression was elevated during glucose starvation, leading to the promotion of phosphoenolpyruvate carboxylase and glucose-6-phosphatase expression in hepatocytes. However, sLZIP knockdown suppressed the expression of the gluconeogenic enzymes under low glucose conditions. sLZIP also enhanced glucose production in the human liver cells and mouse primary hepatic cells. Fasting-induced cyclic adenosine monophosphate impeded sLZIP degradation. Results of glucose and pyruvate tolerance tests showed that sLZIP transgenic mice exhibited abnormal blood glucose metabolism. These findings suggest that sLZIP is a novel regulator of gluconeogenic enzyme expression and plays a role in blood glucose homeostasis during starvation.

A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain

1990 ◽  
Vol 10 (4) ◽  
pp. 1347-1357
Author(s):  
C J Kara ◽  
H C Liou ◽  
L B Ivashkiv ◽  
L H Glimcher
Keyword(s):  
Dna Binding ◽  
Cyclic Amp ◽  
Leucine Zipper ◽  
Binding Protein ◽  
Structural Similarity ◽  
Response Element ◽  
Cellular Genes ◽  
Viral Promoters ◽  
Element Binding Protein ◽  
Cyclic Amp Response Element

The cyclic AMP response element (CRE) is found in many cellular genes regulated by cyclic AMP, and similar elements are present in the early genes of adenovirus that are activated by E1A. The transcription factor CREB has previously been shown to bind this site, and cDNAs for CREB have recently been characterized. We report here the isolation of a cDNA encoding a human DNA-binding protein that also recognizes this motif in cellular and viral promoters. This protein, HB16, displays structural similarity to CREB and to c-Jun and c-Fos, which bind the related 12-O-tetradecanoylphorbol-13-acetate response element (TRE). HB16 contains a highly basic, putative DNA-binding domain and a leucine zipper structure thought to be involved in dimerization. Deletional analysis of HB16 demonstrated that the leucine zipper is required for its interaction with DNA. In addition, HB16 could form a complex with c-Jun but not with c-Fos. Despite its structural similarity to c-Jun and c-Fos and its interaction with c-Jun, HB16 had approximately a 10-fold-lower affinity for the TRE sequence than for the CRE sequence. Although HB16 and CREB both recognized the CRE motif, an extensive binding analysis of HB16 revealed differences in the fine specificity of binding of the two proteins. HB16 mRNA was found at various levels in many human tissues but was most abundant in brain, where its expression was widespread. The existence of more than one CRE-binding protein suggests that the CRE motif could serve multiple regulatory functions.

scholarly journals A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain.

1990 ◽  
Vol 10 (4) ◽  
pp. 1347-1357 ◽  
Author(s):  
C J Kara ◽  
H C Liou ◽  
L B Ivashkiv ◽  
L H Glimcher
Keyword(s):  
Dna Binding ◽  
Cyclic Amp ◽  
Leucine Zipper ◽  
Binding Protein ◽  
Structural Similarity ◽  
Response Element ◽  
Cellular Genes ◽  
Viral Promoters ◽  
Element Binding Protein ◽  
Cyclic Amp Response Element

The cyclic AMP response element (CRE) is found in many cellular genes regulated by cyclic AMP, and similar elements are present in the early genes of adenovirus that are activated by E1A. The transcription factor CREB has previously been shown to bind this site, and cDNAs for CREB have recently been characterized. We report here the isolation of a cDNA encoding a human DNA-binding protein that also recognizes this motif in cellular and viral promoters. This protein, HB16, displays structural similarity to CREB and to c-Jun and c-Fos, which bind the related 12-O-tetradecanoylphorbol-13-acetate response element (TRE). HB16 contains a highly basic, putative DNA-binding domain and a leucine zipper structure thought to be involved in dimerization. Deletional analysis of HB16 demonstrated that the leucine zipper is required for its interaction with DNA. In addition, HB16 could form a complex with c-Jun but not with c-Fos. Despite its structural similarity to c-Jun and c-Fos and its interaction with c-Jun, HB16 had approximately a 10-fold-lower affinity for the TRE sequence than for the CRE sequence. Although HB16 and CREB both recognized the CRE motif, an extensive binding analysis of HB16 revealed differences in the fine specificity of binding of the two proteins. HB16 mRNA was found at various levels in many human tissues but was most abundant in brain, where its expression was widespread. The existence of more than one CRE-binding protein suggests that the CRE motif could serve multiple regulatory functions.

scholarly journals Functional analysis of Met4, a yeast transcriptional activator responsive to S-adenosylmethionine.

1995 ◽  
Vol 15 (1) ◽  
pp. 208-216 ◽  
Author(s):  
L Kuras ◽  
D Thomas
Keyword(s):  
Transcriptional Activation ◽  
Leucine Zipper ◽  
Transcriptional Activator ◽  
Activation Function ◽  
Functional Domain ◽  
Distinct Region ◽  
Activation Domain ◽  
Inhibitory Region ◽  
Leucine Zipper Protein ◽  
Basic Region

Transcription of the genes necessary for sulfur amino acid biosynthesis in Saccharomyces cerevisiae is dependent on Met4, a transcriptional activator that belongs to the basic region-leucine zipper protein family. In this report, we show that one mechanism permitting the repression of the sulfur network by S-adenosylmethionine (AdoMet) involves inhibition of the transcriptional activation function of Met4. Using a wide array of deleted LexA-Met4 fusion proteins as well as various Gal4-Met4 hybrids, we identify the functional domains of Met4 and characterize their relationship. Met4 appears to contain only one activation domain, located in its N-terminal part. We demonstrate that this activation domain functions in a constitutive manner and that AdoMet responsiveness requires a distinct region of Met4. Furthermore, we show that when fused to a heterologous activation domain, this inhibitory region confers inhibition by AdoMet. Met4 contains another distinct functional domain that appears to function as an antagonist of the inhibitory region when intracellular AdoMet is low. On the basis of the presented results, a model for intramolecular regulation of Met4 is proposed.

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