Interactions of The Acidic Domain and SRF Interacting Motifs with the NKX3.1 Homeodomain

Abstract The suppressor of Hairy-wing [su(Hw)] protein mediates the mutagenic effect of the gypsy retrotransposon by repressing the function of transcriptional enhancers located distally from the promoter with respect to the position of the su(Hw)-binding region. Mutations in a second gene, modifier of mdg4, also affect the gypsy-induced phenotype. Two major effects of the mod(mdg4)lul mutation can be distinguished: the interference with insulation by the su(Hw)-binding region and direct inhibition of gene expression that is not dependent on the su(Hw)-binding region position. The mod(mdg4)lul mutation partially suppresses ct6, scD1 and Hw1 mutations, possibly by interfering with the insulation effect of the su(Hw)-binding region. An example of the second effect of mod(mdg4)lul is a complete inactivation of yellow expression in combination with the y 2 allele. Phenotypic analyses of flies with combinations of mod(mdg4)lul and different su(Hw) mutations, or with constructions carrying deletions of the acidic domains of the su(Hw) protein, suggest that the carboxy-terminal acidic domain is important for direct inhibition of yellow transcription in bristles, while the amino-terminal acidic domain is more essential for insulation.

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Mutant p53 Sequestration of the MDM2 Acidic Domain Inhibits E3 Ligase Activity

Molecular and Cellular Biology ◽

10.1128/mcb.00375-18 ◽

2018 ◽

Vol 39 (4) ◽

Cited By ~ 3

Author(s):

Leixiang Yang ◽

Tanjing Song ◽

Qian Cheng ◽

Lihong Chen ◽

Jiandong Chen

Keyword(s):

Tumor Cells ◽

Recent Work ◽

Intramolecular Interaction ◽

E3 Ligase ◽

Mutant P53 ◽

Wild Type ◽

Gain Of Function ◽

Core Domain ◽

Acidic Domain ◽

Wild Type P53

ABSTRACT Missense p53 mutants often accumulate in tumors and drive progression through gain of function. MDM2 efficiently degrades wild-type p53 but fails to degrade mutant p53 in tumor cells. Previous studies revealed that mutant p53 inhibits MDM2 autoubiquitination, suggesting that the interaction inhibits MDM2 E3 activity. Recent work showed that MDM2 E3 activity is stimulated by intramolecular interaction between the RING and acidic domains. Here, we show that in the mutant p53-MDM2 complex, the mutant p53 core domain binds to the MDM2 acidic domain with significantly higher avidity than wild-type p53. The mutant p53-MDM2 complex is deficient in catalyzing ubiquitin release from the activated E2 conjugating enzyme. An MDM2 construct with extra copies of the acidic domain is resistant to inhibition by mutant p53 and efficiently promotes mutant p53 ubiquitination and degradation. The results suggest that mutant p53 interferes with the intramolecular autoactivation mechanism of MDM2, contributing to reduced ubiquitination and increased accumulation in tumor cells.

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The bovine herpesvirus type 1 envelope protein Us9 acidic domain is crucial for anterograde axonal transport

Veterinary Microbiology ◽

10.1016/j.vetmic.2011.05.012 ◽

2011 ◽

Vol 152 (3-4) ◽

pp. 270-279 ◽

Cited By ~ 6

Author(s):

S.I. Chowdhury ◽

M.C.S. Brum ◽

C. Coats ◽

A. Doster ◽

Huiyong Wei ◽

...

Keyword(s):

Axonal Transport ◽

Envelope Protein ◽

Bovine Herpesvirus ◽

Herpesvirus Type ◽

Acidic Domain ◽

Anterograde Axonal Transport ◽

Bovine Herpesvirus Type 1

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Comparative Analysis of 22 Coronavirus HKU1 Genomes Reveals a Novel Genotype and Evidence of Natural Recombination in Coronavirus HKU1

Journal of Virology ◽

10.1128/jvi.00509-06 ◽

2006 ◽

Vol 80 (14) ◽

pp. 7136-7145 ◽

Cited By ~ 125

Author(s):

Patrick C. Y. Woo ◽

Susanna K. P. Lau ◽

Cyril C. Y. Yip ◽

Yi Huang ◽

Hoi-Wah Tsoi ◽

...

Keyword(s):

Respiratory Tract Infections ◽

Single Gene ◽

Human Infection ◽

Bootscan Analysis ◽

Acidic Domain ◽

Multiple Alignments ◽

Genotype C ◽

Natural Recombination ◽

Tract Infections ◽

Genotype A

ABSTRACT We sequenced and compared the complete genomes of 22 strains of coronavirus HKU1 (CoV HKU1) obtained from nasopharyngeal aspirates of patients with respiratory tract infections over a 2-year period. Phylogenetic analysis of 24 putative proteins and polypeptides showed that the 22 CoV HKU1 strains fell into three clusters (genotype A, 13 strains; genotype B, 3 strains and genotype C, 6 strains). However, different phylogenetic relationships among the three clusters were observed in different regions of their genomes. From nsp4 to nsp6, the genotype A strains were clustered with the genotype B strains. For nsp7 and nsp8 and from nsp10 to nsp16, the genotype A strains were clustered with the genotype C strains. From hemagglutinin esterase (HE) to nucleocapsid (N), the genotype B strains were clustered closely with the genotype C strains. Bootscan analysis showed possible recombination between genotypes B and C from nucleotide positions 11500 to 13000, corresponding to the nsp6-nsp7 junction, giving rise to genotype A, and between genotypes A and B from nucleotide positions 21500 to 22500, corresponding to the nsp16-HE junction, giving rise to genotype C. Multiple alignments further narrowed the sites of crossover to a 143-bp region between nucleotide positions 11750 and 11892 and a 29-bp region between nucleotide positions 21502 and 21530. Genome analysis also revealed various numbers of tandem copies of a perfect 30-base acidic tandem repeat (ATR) which encodes NDDEDVVTGD and various numbers and sequences of imperfect repeats in the N terminus of nsp3 inside the acidic domain upstream of papain-like protease 1 among the 22 genomes. All 10 CoV HKU1 strains with incomplete imperfect repeats (1.4 and 4.4) belonged to genotype A. The present study represents the first evidence for natural recombination in coronavirus associated with human infection. Analysis of a single gene is not sufficient for the genotyping of CoV HKU1 strains but requires amplification and sequencing of at least two gene loci, one from nsp10 to nsp16 (e.g., pol or helicase) and another from HE to N (e.g., spike or N). Further studies will delineate whether the ATR is useful for the molecular typing of CoV HKU1.

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A C-Terminal Acidic Domain Regulates Degradation of the Transcriptional Coactivator Bob1

Molecular and Cellular Biology ◽

10.1128/mcb.01590-12 ◽

2013 ◽

Vol 33 (23) ◽

pp. 4628-4640 ◽

Cited By ~ 6

Author(s):

J. M. Lindner ◽

C. S. F. Wong ◽

A. Moller ◽

P. J. Nielsen

Keyword(s):

Transcriptional Coactivator ◽

Acidic Domain

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The Carboxyl-Terminal Region of Human Cytomegalovirus IE1491aa Contains an Acidic Domain That Plays a Regulatory Role and a Chromatin-Tethering Domain That Is Dispensable during Viral Replication

Journal of Virology ◽

10.1128/jvi.79.1.225-233.2005 ◽

2005 ◽

Vol 79 (1) ◽

pp. 225-233 ◽

Cited By ~ 27

Author(s):

Jens Reinhardt ◽

Geoffrey B. Smith ◽

Christopher T. Himmelheber ◽

Jane Azizkhan-Clifford ◽

Edward S. Mocarski

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Human Cytomegalovirus ◽

Deletion Mutant ◽

Viral Gene Expression ◽

Mutant Virus ◽

Serine Phosphorylation ◽

Viral Gene ◽

Acidic Domain ◽

Carboxyl Terminal

ABSTRACT The human cytomegalovirus major immediate-early (α) protein IE1491aa plays an important role in controlling viral gene expression at low multiplicities of infection. With a transient complementation assay, full-length IE1491aa enhanced the growth of ie1 mutant virus CR208 20-fold better than a deletion mutant lacking 71 carboxyl-terminal amino acids (IE11-420aa). A 16-amino-acid domain between amino acids 476 and 491 was both necessary and sufficient for chromatin-tethering activity; however, this domain was completely dispensable for complementation of CR208 replication. The proximal 55-amino-acid acidic domain (amino acids 421 to 475) was found to be most important for function. A deletion mutant lacking only this domain retained chromatin-tethering activity but failed to complement mutant virus. Interestingly, serine phosphorylation (at amino acids 399, 402, 406, 423, 428, 431, 448, 451, and 455) was not required for complementation. These results show that IE1491aa is composed of at least two domains that support replication, a region located between amino acids 1 and 399 that complements ie1 mutant virus replication to low levels and an acidic domain between amino acids 421 and 479 that dramatically enhances complementation.

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Purification of small-size acidic proteoglycan-like domain of carbonic anhydrase IX fused with thioredoxine expressed in Escherichia coli for structural characterization

Biologia ◽

10.1515/biolog-2017-0156 ◽

2017 ◽

Vol 72 (11) ◽

Author(s):

Stanislava Bírová ◽

Zdenko Levarski ◽

Ivana Vidličková ◽

Silvia Pastoreková ◽

Ján Turňa ◽

...

Keyword(s):

Carbonic Anhydrase ◽

Expression System ◽

Carbonic Anhydrase Ix ◽

Its Sequence ◽

Fusion Partner ◽

Aromatic Residues ◽

Acidic Domain ◽

Ca Ix ◽

Acidic Amino Acids ◽

Unusual Amino Acid

AbstractProteoglycan-like (PG) domain of carbonic anhydrase IX (CA IX) is a small-sized acidic domain (8.3 kDa; pI ∼ 3.5) with a very unusual amino acid composition. More than one third of its sequence consists of acidic amino acids and it contains no aromatic residues. It has been revealed that it holds one of the key roles in oncogenetic mechanisms, in which CA IX participates. However, it has not been structurally characterized yet. With these prospects, we developed an expression system of recombinant PG domain production in the form of a fusion protein using thioredoxine (Trx) as the fusion partner in

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