scholarly journals Deletion of the N-Terminal Domain Alters the Ethanol Inhibition ofN-Methyl-d-Aspartate Receptors in a Subunit-Dependent Manner

2013 ◽  
Vol 37 (11) ◽  
pp. 1882-1890 ◽  
Author(s):  
Corigan T. Smothers ◽  
Chun Jin ◽  
John J. Woodward
Keyword(s):  
Dependent Manner ◽  
Ethanol Inhibition ◽  
Terminal Domain ◽  
A Subunit

CAM Kinase IIγ Inhibits Activity and Directly Binds the C-Terminal Domain of the Intestinal Brush Border Na/H Exchanger NHE3 in a Dymanic, Ca2+ Dependent Manner

2011 ◽  
Vol 140 (5) ◽  
pp. S-133
Author(s):  
Mirza Zizak ◽  
Rafiquel Sarker ◽  
Tian-e Chen ◽  
Boyoung Cha ◽  
Marjan Gucek ◽  
...  
Keyword(s):  
Brush Border ◽  
Dependent Manner ◽  
Cam Kinase ◽  
Terminal Domain ◽  
Intestinal Brush Border

Leishmania major biotin protein ligase forms a unique cross-handshake dimer

2021 ◽  
Vol 77 (4) ◽  
pp. 510-521
Author(s):  
Manoj Kumar Rajak ◽  
Sonika Bhatnagar ◽  
Shubhant Pandey ◽  
Sunil Kumar ◽  
Shalini Verma ◽  
...  
Keyword(s):  
Leishmania Major ◽  
Size Exclusion ◽  
Covalent Attachment ◽  
Mitochondrial Enzymes ◽  
Dependent Manner ◽  
Post Translational Modification ◽  
Terminal Domain ◽  
Exclusion Chromatography ◽  
Partial Unfolding ◽  
Biotin Protein Ligase

Biotin protein ligase catalyses the post-translational modification of biotin carboxyl carrier protein (BCCP) domains, a modification that is crucial for the function of several carboxylases. It is a two-step process that results in the covalent attachment of biotin to the ɛ-amino group of a conserved lysine of the BCCP domain of a carboxylase in an ATP-dependent manner. In Leishmania, three mitochondrial enzymes, acetyl-CoA carboxylase, methylcrotonyl-CoA carboxylase and propionyl-CoA carboxylase, depend on biotinylation for activity. In view of the indispensable role of the biotinylating enzyme in the activation of these carboxylases, crystal structures of L. major biotin protein ligase complexed with biotin and with biotinyl-5′-AMP have been solved. L. major biotin protein ligase crystallizes as a unique dimer formed by cross-handshake interactions of the hinge region of the two monomers formed by partial unfolding of the C-terminal domain. Interestingly, the substrate (BCCP domain)-binding site of each monomer is occupied by its own C-terminal domain in the dimer structure. This was observed in all of the crystals that were obtained, suggesting a closed/inactive conformation of the enzyme. Size-exclusion chromatography studies carried out using high protein concentrations (0.5 mM) suggest the formation of a concentration-dependent dimer that exists in equilibrium with the monomer.

scholarly journals The pivot point arginines identified in the β-pinwheel structure of C-terminal domain from Salmonella Typhi DNA Gyrase A subunit

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Ekta Sachdeva ◽  
Gurpreet Kaur ◽  
Pragya Tiwari ◽  
Deepali Gupta ◽  
Tej P. Singh ◽  
...  
Keyword(s):  
Dna Gyrase ◽  
Salmonella Typhi ◽  
Pivot Point ◽  
Terminal Domain ◽  
Gyrase A ◽  
A Subunit

scholarly journals Structural and functional analyses of the N-terminal domain of the A subunit of aBacillus megateriumspore germinant receptor

2019 ◽  
Vol 116 (23) ◽  
pp. 11470-11479 ◽  
Author(s):  
Yunfeng Li ◽  
Kai Jin ◽  
Abigail Perez-Valdespino ◽  
Kyle Federkiewicz ◽  
Andrew Davis ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Abc Transporters ◽  
Spore Germination ◽  
Critical Role ◽  
Chemical Shift Perturbation ◽  
Terminal Domain ◽  
Proposed Model ◽  
Strong Homology ◽  
A Subunit ◽  
Functional Analyses

Germination ofBacillusspores is induced by the interaction of specific nutrient molecules with germinant receptors (GRs) localized in the spore’s inner membrane. GRs typically consist of three subunits referred to as A, B, and C, although functions of individual subunits are not known. Here we present the crystal structure of the N-terminal domain (NTD) of the A subunit of theBacillus megateriumGerK3GR, revealing two distinct globular subdomains bisected by a cleft, a fold with strong homology to substrate-binding proteins in bacterial ABC transporters. Molecular docking, chemical shift perturbation measurement, and mutagenesis coupled with spore germination analyses support a proposed model that the interface between the two subdomains in the NTD of GR A subunits serves as the germinant binding site and plays a critical role in spore germination. Our findings provide a conceptual framework for understanding the germinant recruitment mechanism by which GRs trigger spore germination.

scholarly journals The m6A reader YTHDF1 promotes ovarian cancer progression via augmenting EIF3C translation

2020 ◽  
Vol 48 (7) ◽  
pp. 3816-3831 ◽  
Author(s):  
Tao Liu ◽  
Qinglv Wei ◽  
Jing Jin ◽  
Qingya Luo ◽  
Yi Liu ◽  
...  
Keyword(s):  
Ovarian Cancer ◽  
Cancer Patients ◽  
Cancer Progression ◽  
Protein Translation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Rna Modification ◽  
Dependent Manner ◽  
The Novel ◽  
A Subunit

Abstract N 6-Methyladenosine (m6A) is the most abundant RNA modification in mammal mRNAs and increasing evidence suggests the key roles of m6A in human tumorigenesis. However, whether m6A, especially its ‘reader’ YTHDF1, targets a gene involving in protein translation and thus affects overall protein production in cancer cells is largely unexplored. Here, using multi-omics analysis for ovarian cancer, we identified a novel mechanism involving EIF3C, a subunit of the protein translation initiation factor EIF3, as the direct target of the YTHDF1. YTHDF1 augments the translation of EIF3C in an m6A-dependent manner by binding to m6A-modified EIF3C mRNA and concomitantly promotes the overall translational output, thereby facilitating tumorigenesis and metastasis of ovarian cancer. YTHDF1 is frequently amplified in ovarian cancer and up-regulation of YTHDF1 is associated with the adverse prognosis of ovarian cancer patients. Furthermore, the protein but not the RNA abundance of EIF3C is increased in ovarian cancer and positively correlates with the protein expression of YTHDF1 in ovarian cancer patients, suggesting modification of EIF3C mRNA is more relevant to its role in cancer. Collectively, we identify the novel YTHDF1-EIF3C axis critical for ovarian cancer progression which can serve as a target to develop therapeutics for cancer treatment.

scholarly journals Efg1-mediated Recruitment of NuA4 to Promoters Is Required for Hypha-specific Swi/Snf Binding and Activation inCandida albicans

2008 ◽  
Vol 19 (10) ◽  
pp. 4260-4272 ◽  
Author(s):  
Yang Lu ◽  
Chang Su ◽  
Xuming Mao ◽  
Prashna Pala Raniga ◽  
Haoping Liu ◽  
...  
Keyword(s):  
Chromatin Remodeling ◽  
Transcriptional Activation ◽  
Chromatin Immunoprecipitation ◽  
Pathogenic Fungus ◽  
Dependent Manner ◽  
Hyphal Development ◽  
Chromatin Remodeling Complex ◽  
A Subunit ◽  
Human Pathogenic Fungus ◽  
Incandida Albicans

Efg1 is essential for hyphal development and virulence in the human pathogenic fungus Candida albicans. How Efg1 regulates gene expression is unknown. Here, we show that Efg1 interacts with components of the nucleosome acetyltransferase of H4 (NuA4) histone acetyltransferase (HAT) complex in both yeast and hyphal cells. Deleting YNG2, a subunit of the NuA4 HAT module, results in a significant decrease in the acetylation level of nucleosomal H4 and a profound defect in hyphal development, as well as a defect in the expression of hypha-specific genes. Using chromatin immunoprecipitation, Efg1 and the NuA4 complex are found at the UAS regions of hypha-specific genes in both yeast and hyphal cells, and Efg1 is required for the recruitment of NuA4. Nucleosomal H4 acetylation at the promoters peaks during initial hyphal induction in an Efg1-dependent manner. We also find that Efg1 bound to the promoters of hypha-specific genes is critical for recruitment of the Swi/Snf chromatin remodeling complex during hyphal induction. Our data show that the recruitment of the NuA4 complex by Efg1 to the promoters of hypha-specific genes is required for nucleosomal H4 acetylation at the promoters during hyphal induction and for subsequent binding of Swi/Snf and transcriptional activation.

scholarly journals ARF-like Protein 16 (ARL16) Inhibits RIG-I by Binding with Its C-terminal Domain in a GTP-dependent Manner

2011 ◽  
Vol 286 (12) ◽  
pp. 10568-10580 ◽  
Author(s):  
Yong-Kang Yang ◽  
Hong Qu ◽  
Dong Gao ◽  
Wei Di ◽  
Hai-Wei Chen ◽  
...  
Keyword(s):  
Family Member ◽  
Sendai Virus ◽  
Rna Virus ◽  
Cell Types ◽  
Type I ◽  
Dependent Manner ◽  
Homologous Proteins ◽  
Downstream Signaling ◽  
Terminal Domain ◽  
Inhibitory Function

Retinoic acid-inducible gene I (RIG-I) recognizes RNA virus-derived nucleic acids, which leads to the production of type I interferon (IFN) in most cell types. Tight regulation of RIG-I activity is important to prevent ultra-immune responses. In this study, we identified an ARF-like (ARL) family member, ARL16, as a protein that interacts with RIG-I. Overexpression of ARL16, but not its homologous proteins ARL1 and ARF1, inhibited RIG-I-mediated downstream signaling and antiviral activity. Knockdown of endogenous ARL16 by RNAi potentiated Sendai virus-induced IFN-β expression and vesicular stomatitis virus replication. ARL16 interacted with the C-terminal domain (CTD) of RIG-I to suppress the association between RIG-I and RNA. ARL16 (T37N) and ARL16Δ45–54, which were restricted to the GTP-disassociated form, did not interact with RIG-I and also lost the inhibitory function. Furthermore, we suggest that endogenous ARL16 changes to GTP binding status upon viral infection and binds with the RIG-I CTD to negatively control its signaling activity. These findings suggested a novel innate immune function for an ARL family member, and a GTP-dependent model in which RIG-I is regulated.

scholarly journals The key DNA-binding residues in the C-terminal domain of Mycobacterium tuberculosis DNA gyrase A subunit (GyrA)

2006 ◽  
Vol 34 (19) ◽  
pp. 5650-5659 ◽  
Author(s):  
You-Yi Huang ◽  
Jiao-Yu Deng ◽  
Jing Gu ◽  
Zhi-Ping Zhang ◽  
Anthony Maxwell ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Dna Binding ◽  
Dna Gyrase ◽  
Terminal Domain ◽  
Gyrase A ◽  
A Subunit ◽  
Binding Residues

scholarly journals Transcriptional Adaptor ADA3 of Drosophila melanogaster Is Required for Histone Modification, Position Effect Variegation, and Transcription

2007 ◽  
Vol 28 (1) ◽  
pp. 376-385 ◽  
Author(s):  
Benjamin Grau ◽  
Cristina Popescu ◽  
Laura Torroja ◽  
Daniel Ortuño-Sahagún ◽  
Imre Boros ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Histone Acetyltransferase ◽  
Gene Dosage ◽  
Position Effect ◽  
Position Effect Variegation ◽  
Dependent Manner ◽  
Histone H4 ◽  
Chromosomal Pairing ◽  
Effect Variegation ◽  
A Subunit

ABSTRACT The Drosophila melanogaster gene diskette (also known as dik or dAda3) encodes a protein 29% identical to human ADA3, a subunit of GCN5-containing histone acetyltransferase (HAT) complexes. The fly dADA3 is a major contributor to oogenesis, and it is also required for somatic cell viability. dADA3 localizes to chromosomes, and it is significantly reduced in dGcn5 and dAda2a, but not in dAda2b, mutant backgrounds. In dAda3 mutants, acetylation at histone H3 K9 and K14, but not K18, and at histone H4 K12, but not K5, K8, and K16, is significantly reduced. Also, phosphorylation at H3 S10 is reduced in dAda3 and dGcn5 mutants. Variegation for white (w m4 ) and scute (Hw v ) genes, caused by rearrangements of X chromosome heterochromatin, is modified in a dAda3 + gene-dosage-dependent manner. The effect is not observed with rearrangements involving Y heterochromatin (bw D ), euchromatin (Scutoid), or transvection effects on chromosomal pairing (white and zeste interaction). Activity of scute gene enhancers, targets for Iroquoi transcription factors, is abolished in dAda3 mutants. Also, Iroquoi-associated phenotypes are sensitive to dAda3 + gene dosage. We conclude that dADA3 plays a role in HAT complexes which acetylate H3 and H4 at specific residues. In turn, this acetylation results in chromatin structure effects of certain rearrangements and transcription of specific genes.

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