Studies on gene structure, enzymatic activity and regulatory mechanism of acetohydroxy acid isomeroreductase from G2 pea

2003 ◽  
Vol 46 (4) ◽  
pp. 389 ◽  
Author(s):  
Yunjian XU
Keyword(s):  
Enzymatic Activity ◽  
Gene Structure ◽  
Regulatory Mechanism ◽  
G2 Pea

scholarly journals Genome-Wide Analysis of the FABP Gene Family in Liver of Chicken (Gallus gallus): Identification,Dynamic Expression Profile, and RegulatoryMechanism

2019 ◽  
Vol 20 (23) ◽  
pp. 5948 ◽  
Author(s):  
Wang ◽  
Yue ◽  
Liu ◽  
Yang ◽  
Li ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Gene Family ◽  
Expression Profile ◽  
Gene Structure ◽  
Regulatory Mechanism ◽  
Fatty Acid Binding ◽  
Pparγ Agonist ◽  
Ppar Agonists ◽  
Pparγ Agonists ◽  
Fabp Gene

The fatty acid-binding protein (FABP) gene family, which encodes a group of fatty acid-trafficking molecules that affect cellular functions, has been studied extensively in mammals. However, little is known about the gene structure, expression profile, and regulatory mechanism of the gene family in chickens. In the present study, bioinformatics-based methods were used to identify the family members and investigate their evolutionary history and features of gene structure. Real-time PCR combined with in vivo and in vitro experiments were used to examine the spatiotemporal expression pattern, and explore the regulatory mechanism of FABP genes. The results show that nine members of the FABP gene family, which branched into two clusters and shared a conserved FATTYACIDBP domain, exist in the genome of chickens. Of these, seven FABP genes, including FABP1, FABP3-7, and FABP10 were abundantly expressed in the liver of hens. The expression levels of FABP1, FABP3, and FABP10 were significantly increased, FABP5 and FABP7 were significantly decreased, and FABP4 and FABP6 remained unchanged in hens at the peak laying stage in comparison to those at the pre-laying stage. Transcription of FABP1 and FABP3 were activated by estrogen via estrogen receptor (ER) α, whilst FABP10 was activated by estrogen via ERβ. Meanwhile, the expression of FABP1 was regulated by peroxisome proliferator activated receptor (PPAR) isoforms, of which tested PPARα and PPARβ agonists significantly inhibited the expression of FABP1, while tested PPARγ agonists significantly increased the expression of FABP1, but downregulated it when the concentration of the PPARγ agonist reached 100 nM. The expression of FABP3 was upregulated via tested PPARβ and PPARγ agonists, and the expression of FABP7 was selectively promoted via PPARγ. The expression of FABP10 was activated by all of the three tested PPAR agonists, but the expression of FABP4-6 was not affected by any of the PPAR agonists. In conclusion, members of the FABP gene family in chickens shared similar functional domains, gene structures, and evolutionary histories with mammalian species, but exhibited varying expression profiles and regulatory mechanisms. The results provide a valuable resource for better understanding the biological functions of individual FABP genes in chickens.

scholarly journals A gut-specific chitinase from the mulberry longicorn beetle, Apriona germari (Coleoptera: Cerambycidae): cDNA cloning, gene structure, expression and enzymatic activity

2007 ◽  
Vol 104 (2) ◽  
pp. 173-180 ◽  
Author(s):  
Young Moo CHOO ◽  
Kwang Sik LEE ◽  
Bo Yeon KIM ◽  
Doh Hoon KIM ◽  
Hyung Joo YOON ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Cdna Cloning ◽  
Gene Structure ◽  
Longicorn Beetle

scholarly journals Negative allosteric regulation of Enterococcus faecalis small alarmone synthetase RelQ by single-stranded RNA

2017 ◽  
Vol 114 (14) ◽  
pp. 3726-3731 ◽  
Author(s):  
Jelena Beljantseva ◽  
Pavel Kudrin ◽  
Liis Andresen ◽  
Victoria Shingler ◽  
Gemma C. Atkinson ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Enterococcus Faecalis ◽  
Rna Binding ◽  
Regulatory Mechanism ◽  
Allosteric Regulation ◽  
Rna Binding Protein ◽  
Growth Stress ◽  
Stress Adaptation ◽  
Single Protein ◽  
Allosteric Activator

The alarmone nucleotides guanosine pentaphosphate (pppGpp) and tetraphosphate (ppGpp), collectively referred to as (p)ppGpp, are key regulators of bacterial growth, stress adaptation, pathogenicity, and antibiotic tolerance. We show that the tetrameric small alarmone synthetase (SAS) RelQ from the Gram-positive pathogen Enterococcus faecalis is a sequence-specific RNA-binding protein. RelQ’s enzymatic and RNA binding activities are subject to intricate allosteric regulation. (p)ppGpp synthesis is potently inhibited by the binding of single-stranded RNA. Conversely, RelQ’s enzymatic activity destabilizes the RelQ:RNA complex. pppGpp, an allosteric activator of the enzyme, counteracts the effect of RNA. Tetramerization of RelQ is essential for this regulatory mechanism, because both RNA binding and enzymatic activity are abolished by deletion of the SAS-specific C-terminal helix 5α. The interplay of pppGpp binding, (p)ppGpp synthesis, and RNA binding unites two archetypal regulatory paradigms within a single protein. The mechanism is likely a prevalent but previously unappreciated regulatory switch used by the widely distributed bacterial SAS enzymes.

scholarly journals Regulatory Mechanism of Matrix Metalloprotease-2 Enzymatic Activity by Factor Xa and Thrombin

2009 ◽  
Vol 284 (35) ◽  
pp. 23375-23385 ◽  
Author(s):  
Bon-Hun Koo ◽  
Michael Y. Park ◽  
Ok-Hee Jeon ◽  
Doo-Sik Kim
Keyword(s):  
Enzymatic Activity ◽  
Regulatory Mechanism ◽  
Factor Xa ◽  
Matrix Metalloprotease

Gene structure and enzymatic activity of mouse eosinophil-associated ribonuclease 2

Gene ◽  
2001 ◽  
Vol 267 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Amanda L. McDevitt ◽  
Madeleine S. Deming ◽  
Helene F. Rosenberg ◽  
Kimberly D. Dyer
Keyword(s):  
Enzymatic Activity ◽  
Gene Structure

scholarly journals Tubulin Acetyltransferase αTAT1 Destabilizes Microtubules Independently of Its Acetylation Activity

2012 ◽  
Vol 33 (6) ◽  
pp. 1114-1123 ◽  
Author(s):  
Nereo Kalebic ◽  
Concepcion Martinez ◽  
Emerald Perlas ◽  
Philip Hublitz ◽  
Daniel Bilbao-Cortes ◽  
...  
Keyword(s):  
Enzymatic Activity ◽  
Posttranslational Modification ◽  
Functional Significance ◽  
Mammalian Cells ◽  
Regulatory Mechanism ◽  
Critical Factor ◽  
Cellular Functions ◽  
Microtubule Stability ◽  
Per Se ◽  
Major Target

Acetylation of α-tubulin at lysine 40 (K40) is a well-conserved posttranslational modification that marks long-lived microtubules but has poorly understood functional significance. Recently, αTAT1, a member of the Gcn5-relatedN-acetyltransferase superfamily, has been identified as an α-tubulin acetyltransferase in ciliated organisms. Here, we explored the function of αTAT1 with the aim of understanding the consequences of αTAT1-mediated microtubule acetylation. We demonstrate that α-tubulin is the major target of αTAT1 but that αTAT1 also acetylates itself in a regulatory mechanism that is required for effective modification of tubulin. We further show that in mammalian cells, αTAT1 promotes microtubule destabilization and accelerates microtubule dynamics. Intriguingly, this effect persists in an αTAT1 mutant with no acetyltransferase activity, suggesting that interaction of αTAT1 with microtubules, rather than acetylationper se, is the critical factor regulating microtubule stability. Our data demonstrate that αTAT1 has cellular functions that extend beyond its classical enzymatic activity as an α-tubulin acetyltransferase.

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