keyword
MENU ▼
Read by QxMD icon Read
search

H Jane Dyson

keyword
https://www.readbyqxmd.com/read/27699893/mapping-the-interactions-of-adenoviral-e1a-proteins-with-the-p160-nuclear-receptor-coactivator-binding-domain-of-cbp
#1
Peter Haberz, Munehito Arai, Maria A Martinez-Yamout, H Jane Dyson, Peter E Wright
Many viruses deregulate the cell and force transcription of viral genes by competing with cellular proteins for binding to the transcriptional co-activators CREB-binding protein (CBP) and p300. Through its interactions with CBP/p300 and the retinoblastoma protein, the adenovirus (AdV) early region 1A (E1A) oncoprotein hijacks the cell cycle and, in rodents, transforms the cell; the mechanistic and structural basis for these effects remain unclear. In this study we compare the affinity of protein constructs from the E1A proteins from two adenovirus serotypes, non-oncogenic AdV5 and highly oncogenic AdV12, for binding to the nuclear receptor coactivator binding domain (NCBD) of CBP...
December 2016: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/27387657/finding-our-way-in-the-dark-proteome
#2
Asmit Bhowmick, David H Brookes, Shane R Yost, H Jane Dyson, Julie D Forman-Kay, Daniel Gunter, Martin Head-Gordon, Gregory L Hura, Vijay S Pande, David E Wemmer, Peter E Wright, Teresa Head-Gordon
The traditional structure-function paradigm has provided significant insights for well-folded proteins in which structures can be easily and rapidly revealed by X-ray crystallography beamlines. However, approximately one-third of the human proteome is comprised of intrinsically disordered proteins and regions (IDPs/IDRs) that do not adopt a dominant well-folded structure, and therefore remain "unseen" by traditional structural biology methods. This Perspective considers the challenges raised by the "Dark Proteome", in which determining the diverse conformational substates of IDPs in their free states, in encounter complexes of bound states, and in complexes retaining significant disorder requires an unprecedented level of integration of multiple and complementary solution-based experiments that are analyzed with state-of-the art molecular simulation, Bayesian probabilistic models, and high-throughput computation...
August 10, 2016: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/27249581/the-dependence-of-carbohydrate-aromatic-interaction-strengths-on-the-structure-of-the-carbohydrate
#3
Che-Hsiung Hsu, Sangho Park, David E Mortenson, B Lachele Foley, Xiaocong Wang, Robert J Woods, David A Case, Evan T Powers, Chi-Huey Wong, H Jane Dyson, Jeffery W Kelly
Interactions between proteins and carbohydrates are ubiquitous in biology. Therefore, understanding the factors that determine their affinity and selectivity are correspondingly important. Herein, we have determined the relative strengths of intramolecular interactions between a series of monosaccharides and an aromatic ring close to the glycosylation site in an N-glycoprotein host. We employed the enhanced aromatic sequon, a structural motif found in the reverse turns of some N-glycoproteins, to facilitate face-to-face monosaccharide-aromatic interactions...
June 22, 2016: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/27185953/structural-characterization-of-the-ternary-complex-that-mediates-termination-of-nf-%C3%AE%C2%BAb-signaling-by-i%C3%AE%C2%BAb%C3%AE
#4
Sulakshana P Mukherjee, Pedro O Quintas, Reginald McNulty, Elizabeth A Komives, H Jane Dyson
The transcription factor NF-κB is used in many systems for the transduction of extracellular signals into the expression of signal-responsive genes. Published structural data explain the activation of NF-κB through degradation of its dedicated inhibitor IκBα, but the mechanism by which NF-κB-mediated signaling is turned off by its removal from the DNA in the presence of newly synthesized IκBα (termed stripping) is unknown. Previous kinetic studies showed that IκBα accelerates NF-κB dissociation from DNA, and a transient ternary complex between NF-κB, its cognate DNA sequence, and IκBα was observed...
May 31, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/26976603/recognition-of-the-disordered-p53-transactivation-domain-by-the-transcriptional-adapter-zinc-finger-domains-of-creb-binding-protein
#5
Alexander S Krois, Josephine C Ferreon, Maria A Martinez-Yamout, H Jane Dyson, Peter E Wright
An important component of the activity of p53 as a tumor suppressor is its interaction with the transcriptional coactivators cyclic-AMP response element-binding protein (CREB)-binding protein (CBP) and p300, which activate transcription of p53-regulated stress response genes and stabilize p53 against ubiquitin-mediated degradation. The highest affinity interactions are between the intrinsically disordered N-terminal transactivation domain (TAD) of p53 and the TAZ1 and TAZ2 domains of CBP/p300. The NMR spectra of simple binary complexes of the TAZ1 and TAZ2 domains with the p53TAD suffer from exchange broadening, but innovations in construct design and isotopic labeling have enabled us to obtain high-resolution structures using fusion proteins, uniformly labeled in the case of the TAZ2-p53TAD fusion and segmentally labeled through transintein splicing for the TAZ1-p53TAD fusion...
March 29, 2016: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/26958875/making-sense-of-intrinsically-disordered-proteins
#6
REVIEW
H Jane Dyson
No abstract text is available yet for this article.
March 8, 2016: Biophysical Journal
https://www.readbyqxmd.com/read/26647230/nmr-characterization-of-a-72-kda-transcription-factor-using-differential-isotopic-labeling
#7
Sulakshana P Mukherjee, Brendan Borin, Pedro O Quintas, H Jane Dyson
NF-κB is a major transcription factor that mediates a number of cellular signaling pathways. Crystal structure analysis gives an incomplete picture of the behavior of the protein, particularly in the free state; free monomers or dimers of NF-κB have never been crystallized. NMR analysis gives insights into the structure and dynamics of the protein in solution, but a necessary first step is the assignment of resonances. The size of the heterodimer of the Rel homology regions of the NF-κB monomers p65 and p50 (72 kDa) prohibits the straightforward use of triple-resonance spectroscopy to obtain the assignments...
March 2016: Protein Science: a Publication of the Protein Society
https://www.readbyqxmd.com/read/26377787/biomolecular-systems-interactions-dynamics-and-allostery-reflections-and-new-directions
#8
EDITORIAL
Ozlem Keskin, H Jane Dyson, Ivet Bahar
No abstract text is available yet for this article.
September 15, 2015: Biophysical Journal
https://www.readbyqxmd.com/read/26195786/conformational-propensities-of-intrinsically-disordered-proteins-influence-the-mechanism-of-binding-and-folding
#9
Munehito Arai, Kenji Sugase, H Jane Dyson, Peter E Wright
Intrinsically disordered proteins (IDPs) frequently function in protein interaction networks that regulate crucial cellular signaling pathways. Many IDPs undergo transitions from disordered conformational ensembles to folded structures upon binding to their cellular targets. Several possible binding mechanisms for coupled folding and binding have been identified: folding of the IDP after association with the target ("induced fit"), or binding of a prefolded state in the conformational ensemble of the IDP to the target protein ("conformational selection"), or some combination of these two extremes...
August 4, 2015: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/26147643/cofactor-mediated-conformational-dynamics-promote-product-release-from-escherichia-coli-dihydrofolate-reductase-via-an-allosteric-pathway
#10
David Oyen, R Bryn Fenwick, Robyn L Stanfield, H Jane Dyson, Peter E Wright
The enzyme dihydrofolate reductase (DHFR, E) from Escherichia coli is a paradigm for the role of protein dynamics in enzyme catalysis. Previous studies have shown that the enzyme progresses through the kinetic cycle by modulating the dynamic conformational landscape in the presence of substrate dihydrofolate (DHF), product tetrahydrofolate (THF), and cofactor (NADPH or NADP(+)). This study focuses on the quantitative description of the relationship between protein fluctuations and product release, the rate-limiting step of DHFR catalysis...
July 29, 2015: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/26073260/functional-advantages-of-dynamic-protein-disorder
#11
REVIEW
Rebecca B Berlow, H Jane Dyson, Peter E Wright
Intrinsically disordered proteins participate in many important cellular regulatory processes. The absence of a well-defined structure in the free state of a disordered domain, and even on occasion when it is bound to physiological partners, is fundamental to its function. Disordered domains are frequently the location of multiple sites for post-translational modification, the key element of metabolic control in the cell. When a disordered domain folds upon binding to a partner, the resulting complex buries a far greater surface area than in an interaction of comparably-sized folded proteins, thus maximizing specificity at modest protein size...
September 14, 2015: FEBS Letters
https://www.readbyqxmd.com/read/25531225/intrinsically-disordered-proteins-in-cellular-signalling-and-regulation
#12
REVIEW
Peter E Wright, H Jane Dyson
Intrinsically disordered proteins (IDPs) are important components of the cellular signalling machinery, allowing the same polypeptide to undertake different interactions with different consequences. IDPs are subject to combinatorial post-translational modifications and alternative splicing, adding complexity to regulatory networks and providing a mechanism for tissue-specific signalling. These proteins participate in the assembly of signalling complexes and in the dynamic self-assembly of membrane-less nuclear and cytoplasmic organelles...
January 2015: Nature Reviews. Molecular Cell Biology
https://www.readbyqxmd.com/read/25451029/the-high-risk-hpv16-e7-oncoprotein-mediates-interaction-between-the-transcriptional-coactivator-cbp-and-the-retinoblastoma-protein-prb
#13
Ariane L Jansma, Maria A Martinez-Yamout, Rong Liao, Peiqing Sun, H Jane Dyson, Peter E Wright
The oncoprotein E7 from human papillomavirus (HPV) strains that confer high cancer risk mediates cell transformation by deregulating host cellular processes and activating viral gene expression through recruitment of cellular proteins such as the retinoblastoma protein (pRb) and the cyclic-AMP response element binding binding protein (CBP) and its paralog p300. Here we show that the intrinsically disordered N-terminal region of E7 from high-risk HPV16 binds the TAZ2 domain of CBP with greater affinity than E7 from low-risk HPV6b...
December 12, 2014: Journal of Molecular Biology
https://www.readbyqxmd.com/read/24857522/probing-the-non-native-h-helix-translocation-in-apomyoglobin-folding-intermediates
#14
Phillip C Aoto, Chiaki Nishimura, H Jane Dyson, Peter E Wright
Apomyoglobin folds via sequential helical intermediates that are formed by rapid collapse of the A, B, G, and H helix regions. An equilibrium molten globule with a similar structure is formed near pH 4. Previous studies suggested that the folding intermediates are kinetically trapped states in which folding is impeded by non-native packing of the G and H helices. Fluorescence spectra of mutant proteins in which cysteine residues were introduced at several positions in the G and H helices show differential quenching of W14 fluorescence, providing direct evidence of translocation of the H helix relative to helices A and G in both the kinetic and equilibrium intermediates...
June 17, 2014: Biochemistry
https://www.readbyqxmd.com/read/24843873/intramolecular-polyspecificity-in-cd4-t-cell-recognition-of-ad-restricted-epitopes-of-proteoglycan-aggrecan
#15
Jane Falconer, Katie Lowes, Anna L Furmanski, Julian Dyson, Wan Fai Ng, John H Robinson
T-cell recognition of MHC–peptide complexes shows a high degree of polyspecificity extending to recognition of a large number of structurally unrelated peptides. Examples of polyspecificity reported to date are confined to recognition of epitopes from distinct proteins or synthetic peptide libraries. Here we describe intramolecular polyspecificity of CD4 T cells specific for several epitopes within proteoglycan aggrecan, a structural glycoprotein of cartilage and candidate autoantigen in rheumatoid arthritis...
May 2014: Immunology
https://www.readbyqxmd.com/read/24521053/structural-characterization-of-interactions-between-the-double-stranded-rna-binding-zinc-finger-protein-jaz-and-nucleic-acids
#16
Russell G Burge, Maria A Martinez-Yamout, H Jane Dyson, Peter E Wright
The interactions of the human double-stranded RNA-binding zinc finger protein JAZ with RNA or DNA were investigated using electrophoretic mobility-shift assays, isothermal calorimetry, and nuclear magnetic resonance spectroscopy. Consistent with previous reports, JAZ has very low affinity for duplex DNA or single-stranded RNA, but it binds preferentially to double-stranded RNA (dsRNA) with no detectable sequence specificity. The affinity of JAZ for dsRNA is unaffected by local structural features such as loops, overhangs, and bulges, provided a sufficient length of reasonably well-structured A-form RNA (about 18 bp for a single zinc finger) is present...
March 11, 2014: Biochemistry
https://www.readbyqxmd.com/read/24498949/side-chain-conformational-averaging-in-human-dihydrofolate-reductase
#17
Lisa M Tuttle, H Jane Dyson, Peter E Wright
The three-dimensional structures of the dihydrofolate reductase enzymes from Escherichia coli (ecDHFR or ecE) and Homo sapiens (hDHFR or hE) are very similar, despite a rather low level of sequence identity. Whereas the active site loops of ecDHFR undergo major conformational rearrangements during progression through the reaction cycle, hDHFR remains fixed in a closed loop conformation in all of its catalytic intermediates. To elucidate the structural and dynamic differences between the human and E. coli enzymes, we conducted a comprehensive analysis of side chain flexibility and dynamics in complexes of hDHFR that represent intermediates in the major catalytic cycle...
February 25, 2014: Biochemistry
https://www.readbyqxmd.com/read/24077226/divergent-evolution-of-protein-conformational-dynamics-in-dihydrofolate-reductase
#18
Gira Bhabha, Damian C Ekiert, Madeleine Jennewein, Christian M Zmasek, Lisa M Tuttle, Gerard Kroon, H Jane Dyson, Adam Godzik, Ian A Wilson, Peter E Wright
Molecular evolution is driven by mutations, which may affect the fitness of an organism and are then subject to natural selection or genetic drift. Analysis of primary protein sequences and tertiary structures has yielded valuable insights into the evolution of protein function, but little is known about the evolution of functional mechanisms, protein dynamics and conformational plasticity essential for activity. We characterized the atomic-level motions across divergent members of the dihydrofolate reductase (DHFR) family...
November 2013: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/23831576/the-ch2-domain-of-cbp-p300-is-a-novel-zinc-finger
#19
Sangho Park, Maria A Martinez-Yamout, H Jane Dyson, Peter E Wright
The transcriptional co-regulator CBP (CREB-binding protein) has a highly conserved cysteine/histidine-rich region (CH2) whose structure and function remain uncharacterized. Using nuclear magnetic resonance (NMR spectroscopy), sequence alignment, mass spectrometry, and mutagenesis, we show that the CH2 domain is not a canonical plant homeodomain (PHD) finger, as previously proposed, but binds an additional zinc atom through the region N-terminal to the putative PHD motif. The CH2 domain and the preceding bromodomain interact and mutually stabilize each other, implying a cooperative function...
August 19, 2013: FEBS Letters
https://www.readbyqxmd.com/read/23758161/a-distal-mutation-perturbs-dynamic-amino-acid-networks-in-dihydrofolate-reductase
#20
David D Boehr, Jason R Schnell, Dan McElheny, Sung-Hun Bae, Brendan M Duggan, Stephen J Benkovic, H Jane Dyson, Peter E Wright
Correlated networks of amino acids have been proposed to play a fundamental role in allostery and enzyme catalysis. These networks of amino acids can be traced from surface-exposed residues all the way into the active site, and disruption of these networks can decrease enzyme activity. Substitution of the distal Gly121 residue in Escherichia coli dihydrofolate reductase results in an up to 200-fold decrease in the hydride transfer rate despite the fact that the residue is located 15 Å from the active-site center...
July 9, 2013: Biochemistry
keyword
keyword
76384
1
2
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"