Search results for: H. Jane Dyson

Items from 1 to 20 out of 109 results

article

Mispacking of the F87 sidechain drives aggregation‐promoting conformational fluctuations in the subunit interfaces of the transthyretin tetramer

Xun Sun, James A. Ferguson, Ke Yang, Robyn L. Stanfield, more

Aberrant formation and deposition of human transthyretin (TTR) aggregates causes transthyretin amyloidosis. To initialize aggregation, transthyretin tetramers must first dissociate into monomers that partially unfold to promote entry into the aggregation pathway. The native TTR tetramer (T) is stabilized by docking of the F87 sidechain into an interfacial cavity enclosed by several hydrophobic residues...

article

Comparison of backbone dynamics of the p50 dimerization domain of NFκB in the homodimeric transcription factor NFκB1 and in its heterodimeric complex with RelA (p65)

Bastian Kohl, Vanessa Granitzka, Amrinder Singh, Pedro Quintas, more

Protein Science > 28 > 12 > 2064 - 2072

The nuclear factor of kappa light polypeptide gene enhancer in B‐cells (NFκB) transcription factors play a critical role in human immune response. The family includes homodimers and heterodimers of five component proteins, which mediate different transcriptional responses and bind preferentially to different DNA sequences. Crystal structures of DNA complexes show that the dimers of the Rel‐homology...

article

Aggregation of zinc‐free p53 is inhibited by Hsp90 but not other chaperones

Huiwen Wu, H. Jane Dyson

Protein Science > 28 > 11 > 2020 - 2023

The structured DNA‐binding domain (DBD) of p53 is a well‐known client protein of the chaperone Hsp90. The p53 DBD contains a single zinc ion, coordinated by the side chains of Cys176, His179, Cys238, and Cys242; zinc coordination plays a structural role to stabilize the DBD and is required for its DNA binding. The ambiguous nature of the p53‐Hsp90 interaction, together with the stabilizing role of...

article

Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation

Rebecca B. Berlow, H. Jane Dyson, Peter E. Wright

Journal of Molecular Biology > 2018 > 430 > 16 > 2309-2320

Allosteric regulatory processes are implicated at all levels of biological function. Recent advances in our understanding of the diverse and functionally significant class of intrinsically disordered proteins have identified a multitude of ways in which disordered proteins function within the confines of the allosteric paradigm. Allostery within or mediated by intrinsically disordered proteins ensures...

article

Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP

Peter Haberz, Munehito Arai, Maria A. Martinez‐Yamout, H. Jane Dyson, more

Protein Science > 25 > 12 > 2256 - 2267

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...

chapter

Structure and Function of the CBP/p300 TAZ Domains

Roberto N. Guzman, Maria A. Martinez-Yamout, H. Jane Dyson, Peter E. Wright

Molecular Biology Intelligence Unit > Zinc Finger Proteins > Binding of Zinc Fingers to Proteins > 114-120

The TAZ (transcriptional adapter zinc binding) domains in the transcriptional coactivators CBP/p300 are zinc-binding motifs that are primarily involved in protein-protein recognition. The activation domains of more than 30 transcription factors have been reported to bind to the TAZ domains, and each TAZ domain generally binds a different subset of transcription factors. Structurally, the TAZ domains...

article

Making Sense of Intrinsically Disordered Proteins

H. Jane Dyson

Biophysical Journal > 2016 > 110 > 5 > 1013-1016

article

NMR characterization of a 72 kDa transcription factor using differential isotopic labeling

Sulakshana P. Mukherjee, Brendan Borin, Pedro O. Quintas, H. Jane Dyson

Protein Science > 25 > 3 > 597 - 604

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...

article

Classic Analysis of Biopolymer Dynamics Is Model Free

R. Bryn Fenwick, H. Jane Dyson

Biophysical Journal > 2016 > 110 > 1 > 3-6

Early analysis of biopolymer dynamics relied on a variety of motional models that were difficult to distinguish and sometimes gave contradictory results. The Lipari-Szabo model-free approach (documented in a 1980 article in Biophysical Journal, as well as in two more comprehensive 1982 articles in the Journal of the American Chemical Society, provided a simple formalism that allowed investigators...

article

Biomolecular Systems Interactions, Dynamics, and Allostery: Reflections and New Directions

Ozlem Keskin, H. Jane Dyson, Ivet Bahar

Biophysical Journal > 2015 > 109 > 6 > E1-E2

article

Functional advantages of dynamic protein disorder

Rebecca B. Berlow, H. Jane Dyson, Peter E. Wright

FEBS Letters > 2015 > 589 > 19 Part A > 2433-2440

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...

article

Functional advantages of dynamic protein disorder

Rebecca B. Berlow, H. Jane Dyson, Peter E. Wright

FEBS Letters > 589 > 19PartA > 2433 - 2440

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...

article

The High-Risk HPV16 E7 Oncoprotein Mediates Interaction between the Transcriptional Coactivator CBP and the Retinoblastoma Protein pRb

Ariane L. Jansma, Maria A. Martinez-Yamout, Rong Liao, Peiqing Sun, more

Journal of Molecular Biology > 2014 > 426 > 24 > 4030-4048

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...

article

The CH2 domain of CBP/p300 is a novel zinc finger

Sangho Park, Maria A. Martinez-Yamout, H. Jane Dyson, Peter E. Wright

FEBS Letters > 2013 > 587 > 16 > 2506-2511

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...

article

Localized Structural Fluctuations Promote Amyloidogenic Conformations in Transthyretin

Kwang Hun Lim, H. Jane Dyson, Jeffery W. Kelly, Peter E. Wright

Journal of Molecular Biology > 2013 > 425 > 6 > 977-988

The process of transthyretin (TTR) misfolding and aggregation, including amyloid formation, appears to cause a number of degenerative diseases. During amyloid formation, the native protein undergoes a tetramer-to-folded monomer transition, followed by local unfolding of the monomer to an assembly-competent amyloidogenic intermediate. Here we use NMR relaxation dispersion to probe conformational exchange...

article

Long-Range Effects and Functional Consequences of Stabilizing Mutations in the Ankyrin Repeat Domain of IκBα

Carla F. Cervantes, Lindsey D. Handley, Shih-Che Sue, H. Jane Dyson, more

Journal of Molecular Biology > 2013 > 425 > 5 > 902-913

Protein domains containing three or more ankyrin repeats (ARs) are ubiquitous in all phyla. Sequence alignments previously identified certain conserved positions, which have been shown to stabilize AR domains and promote their folding. Consensus mutations [Y254L/T257A (YLTA) and C186P/A220P (CPAP)] stabilize the naturally occuring AR domain of human IκBα to denaturation; however, only the YLTA mutations...

article

Kaiso uses all three zinc fingers and adjacent sequence motifs for high affinity binding to sequence-specific and methyl-CpG DNA targets

Bethany A. Buck-Koehntop, Maria A. Martinez-Yamout, H. Jane Dyson, Peter E. Wright

FEBS Letters > 2012 > 586 > 6 > 734-739

Kaiso is a Cys ₂ His ₂ zinc finger (ZF) protein that mediates methyl-CpG-dependent and sequence-specific transcriptional repression. As a first step towards elucidating the structural and molecular basis for recognition of these disparate DNA sequences, the minimal binding region of Kaiso was identified and optimal DNA sequences for high-affinity interactions were characterized. Contrary...

article

Solution NMR as an Investigational Tool for Disordered and Partly Folded Proteins

H. Jane Dyson, Sung Jean Park, Jing Zhu, Maria A. Martinez-Yamout

Biophysical Journal > 2012 > 102 > 3 Supplement 1 > 2a

article

CheShift-2 resolves a local inconsistency between two X-ray crystal structures

Jorge A. Vila, Shih-Che Sue, James S. Fraser, Harold A. Scheraga, more

Journal of Biomolecular NMR > 2012 > 54 > 2 > 193-198

Since chemical shifts provide important and relatively accessible information about protein structure in solution, a Web server, CheShift-2, was developed for structure interrogation, based on a quantum mechanics database of ¹³C^α chemical shifts. We report the application of CheShift-2 to a local inconsistency between two X-ray crystal structures (PDB IDs 1IKN and 1NFI) of the complex between the...

article

Dynamic Interaction of Hsp90 with Its Client Protein p53

Sung Jean Park, Milka Kostic, H. Jane Dyson

Journal of Molecular Biology > 2011 > 411 > 1 > 158-173

Although the structure of the molecular chaperone Hsp90 has been extensively characterized by X-ray crystallography, the nature of the interactions between Hsp90 and its client proteins remains unclear. We present results from a series of spectroscopic studies that strongly suggest that these interactions are highly dynamic in solution. Extensive NMR assignments have been made for human Hsp90 through...

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Search results for: H. Jane Dyson

Mispacking of the F87 sidechain drives aggregation‐promoting conformational fluctuations in the subunit interfaces of the transthyretin tetramer

Comparison of backbone dynamics of the p50 dimerization domain of NFκB in the homodimeric transcription factor NFκB1 and in its heterodimeric complex with RelA (p65)

Aggregation of zinc‐free p53 is inhibited by Hsp90 but not other chaperones

Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation

Mapping the interactions of adenoviral E1A proteins with the p160 nuclear receptor coactivator binding domain of CBP

Structure and Function of the CBP/p300 TAZ Domains

Making Sense of Intrinsically Disordered Proteins

NMR characterization of a 72 kDa transcription factor using differential isotopic labeling

Classic Analysis of Biopolymer Dynamics Is Model Free

Biomolecular Systems Interactions, Dynamics, and Allostery: Reflections and New Directions

Functional advantages of dynamic protein disorder

Functional advantages of dynamic protein disorder

The High-Risk HPV16 E7 Oncoprotein Mediates Interaction between the Transcriptional Coactivator CBP and the Retinoblastoma Protein pRb

The CH2 domain of CBP/p300 is a novel zinc finger

Localized Structural Fluctuations Promote Amyloidogenic Conformations in Transthyretin

Long-Range Effects and Functional Consequences of Stabilizing Mutations in the Ankyrin Repeat Domain of IκBα

Kaiso uses all three zinc fingers and adjacent sequence motifs for high affinity binding to sequence-specific and methyl-CpG DNA targets

Solution NMR as an Investigational Tool for Disordered and Partly Folded Proteins

CheShift-2 resolves a local inconsistency between two X-ray crystal structures

Dynamic Interaction of Hsp90 with Its Client Protein p53

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