Role of Important Hydrophobic Amino Acids in the Interaction between the Glucocorticoid Receptor τ1-Core Activation Domain and Target Factors†

Biochemistry ◽  
1998 ◽  
Vol 37 (26) ◽  
pp. 9586-9594 ◽  
Author(s):  
Tova Almlöf ◽  
Annika E. Wallberg ◽  
Jan-Åke Gustafsson ◽  
Anthony P. H. Wright
Keyword(s):  
Amino Acids ◽  
Glucocorticoid Receptor ◽  
Activation Domain ◽  
Hydrophobic Amino Acids

scholarly journals De Novo designed 13 mer hairpin-peptide arrests insulin and inhibits its aggregation: role of OH–π interactions between water and hydrophobic amino acids

RSC Advances ◽  
2020 ◽  
Vol 10 (25) ◽  
pp. 14991-14999
Author(s):  
Meghomukta Mukherjee ◽  
Nilanjan Banerjee ◽  
Subhrangsu Chatterjee
Keyword(s):  
Amino Acids ◽  
Neurodegenerative Diseases ◽  
Type Ii Diabetes ◽  
De Novo ◽  
Prion Diseases ◽  
Cellular Systems ◽  
Type Ii ◽  
P Protein ◽  
Hydrophobic Amino Acids

Protein aggregation in the cellular systems can be highly fatal causing a series of diseases including neurodegenerative diseases like ALS, Alzheimer, Prion Diseases, Parkinson's and other diseases like type II diabetes.

scholarly journals Role of Hydrophobic Amino Acids at β85 and β88 in Stabilizing F Helix Conformation of Hemoglobin S

1996 ◽  
Vol 271 (40) ◽  
pp. 24564-24568 ◽  
Author(s):  
Lattupally R. Reddy ◽  
Konda S. Reddy ◽  
Saul Surrey ◽  
Kazuhiko Adachi
Keyword(s):  
Amino Acids ◽  
Hemoglobin S ◽  
Hydrophobic Amino Acids ◽  
Helix Conformation

scholarly journals Role of conserved hydrophobic amino acids in androgen receptor AF-1 function

2003 ◽  
Vol 31 (3) ◽  
pp. 427-439 ◽  
Author(s):  
R Betney ◽  
IJ McEwan
Keyword(s):  
Amino Acids ◽  
Transcription Factor ◽  
Androgen Receptor ◽  
Gene Transcription ◽  
Hydrophobic Residues ◽  
Steroid Receptor Coactivator ◽  
Binding Interface ◽  
Hydrophobic Amino Acids

The intracellular androgen receptor (AR) is a ligand-activated transcription factor. Upon binding the steroids testosterone or dihydrotestosterone, the activated receptor translocates to the nucleus, binds to specific DNA response elements and interacts with the transcription machinery in order to regulate gene transcription. In the present study, we have described a highly conserved region (amino acids 224-258) within the AR AF-1 domain and have investigated the role of conserved bulky hydrophobic residues in gene regulation. Mutating pairs of residues (I229A/L236A; V240A/V242A; L251A/L254A) reduced transactivation activity by 25-40%. Mutating residues M244, L246 and V248 to alanines had a more dramatic affect on receptor activity, disrupting activity by at least 60%. The latter mutations also disrupted binding to the RNA polymerase-associated protein 74 subunit of the general transcription factor TFIIF. The protein conformation and stability of the mutant polypeptide in vitro was not significantly different from the wild type. None of the mutations tested disrupted binding of the AF-1 domain with the coactivator protein steroid receptor coactivator-1a. Thus we have concluded that conserved hydrophobic residues are important for receptor-dependent gene transcription and that M244, L246 and V248 are part of the binding interface for TFIIF.

scholarly journals The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing.

1995 ◽  
Vol 15 (1) ◽  
pp. 76-86 ◽  
Author(s):  
A Baniahmad ◽  
X Leng ◽  
T P Burris ◽  
S Y Tsai ◽  
M J Tsai ◽  
...  
Keyword(s):  
Amino Acids ◽  
Thyroid Hormone ◽  
Ligand Binding ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
Activation Domain ◽  
C Terminus

The C terminus of nuclear hormone receptors is a complex structure that contains multiple functions. We are interested in the mechanism by which thyroid hormone converts its receptor from a transcriptional silencer to an activator of transcription. Both regulatory functions are localized in the ligand binding domain of this receptor superfamily member. In this study, we have identified and characterized several functional domains within the ligand binding domain of the human thyroid hormone receptor (TR beta) conferring transactivation. Interestingly, these domains are localized adjacent to hormone binding sites. One activation domain, designated tau 4, is only 17 amino acids in length and is localized at the extreme C terminus of TR. Deletion of six amino acids of tau 4 resulted in a receptor that could still bind hormone but acted as a constitutive silencer, indicating that tau 4 is required for both transactivation and relief of the silencing functions. In addition, we performed in vivo competition experiments, the results of which suggest that in the absence of tau 4 or hormone, TR is bound by a corepressor protein(s) and that one role of hormone is to release corepressor from the receptor. We propose a general model in which the role of hormone is to induce a conformational change in the receptor that subsequently affects the action of tau 4, leading to both relief of silencing and transcriptional activation.

scholarly journals Aggregation and Molecular Properties of β-Glucosidase Isoform II in Chayote (Sechium edule)

Molecules ◽  
2020 ◽  
Vol 25 (7) ◽  
pp. 1699
Author(s):  
Alberto Cruz Rodríguez ◽  
Fabiola Anaid Sánchez Esperanza ◽  
Eduardo Pérez-Campos ◽  
María Teresa Hernández-Huerta ◽  
Laura Pérez-Campos Mayoral ◽  
...  
Keyword(s):  
Amino Acids ◽  
Buffer Solution ◽  
Native Page ◽  
Sechium Edule ◽  
Chromatography Tandem Mass Spectrometry ◽  
Sds Page ◽  
Liquid Chromatography Tandem Mass ◽  
Hydrophobic Amino Acids ◽  
Nano Liquid Chromatography

The presence of isoforms of β-glucosidase has been reported in some grasses such as sorghum, rice and maize. This work aims to extract and characterize isoform II in β-glucosidase from S. edule. A crude extract was prepared without buffer solution and adjusted to pH 4.6. Contaminating proteins were precipitated at 4 °C for 24 h. The supernatant was purified by chromatography on carboxymethyl cellulose (CMC) column, molecular exclusion on Sephacryl S-200HR, and exchange anionic on QFF column. Electrophoretic analyzes revealed a purified enzyme with aggregating molecular complex on SDS-PAGE, Native-PAGE, and AU-PAGE. Twelve peptides fragments were identified by nano liquid chromatography-tandem mass spectrometry (nano LC-ESI-MS/MS), which presented as 61% identical to Cucurbita moschata β-glucosidase and 55.74% identical to β-glucosidase from Cucumis sativus, another Cucurbitaceous member. The relative masses which contained 39% hydrophobic amino acids ranged from 982.49 to 2,781.26. The enzyme showed a specificity to β-d-glucose with a Km of 4.59 mM, a Vmax value of 104.3 μM∙min−1 and a kcat of 10,087 μM∙min−1 using p-nitrophenyl-β-D-glucopyranoside. The presence of molecular aggregates can be attributed to non-polar amino acids. This property is not mediated by a β-glucosidase aggregating factor (BGAF) as in grasses (maize and sorghum). The role of these aggregates is discussed.

scholarly journals The expanded specificity and physiological role of a widespread N-degron recognin

2019 ◽  
Vol 116 (37) ◽  
pp. 18629-18637 ◽  
Author(s):  
Xiaohui Gao ◽  
Jinki Yeom ◽  
Eduardo A. Groisman
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Salmonella Enterica ◽  
Physiological Role ◽  
Strong Preference ◽  
Protein Homeostasis ◽  
Intact Proteins ◽  
N Terminus ◽  
Hydrophobic Amino Acids

All cells use proteases to maintain protein homeostasis. The proteolytic systems known as the N-degron pathways recognize signals at the N terminus of proteins and bring about the degradation of these proteins. The ClpS protein enforces the N-degron pathway in bacteria and bacteria-derived organelles by targeting proteins harboring leucine, phenylalanine, tryptophan, or tyrosine at the N terminus for degradation by the protease ClpAP. We now report that ClpS binds, and ClpSAP degrades, proteins still harboring the N-terminal methionine. We determine that ClpS recognizes a type of degron in intact proteins based on the identity of the fourth amino acid from the N terminus, showing a strong preference for large hydrophobic amino acids. We uncover natural ClpS substrates in the bacteriumSalmonella enterica, including SpoT, the essential synthase/hydrolase of the alarmone (p)ppGpp. Our findings expand both the specificity and physiological role of the widespread N-degron recognin ClpS.

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