scholarly journals Differential conformational dynamics in the closely homologous FK506-binding domains of FKBP51 and FKBP52

2014 ◽  
Vol 461 (1) ◽  
pp. 115-123 ◽  
Author(s):  
Sourajit M. Mustafi ◽  
David M. LeMaster ◽  
Griselda Hernández
Keyword(s):  
Conformational Dynamics ◽  
Steroid Receptor ◽  
Receptor Activity ◽  
Binding Domains

Unlike FKBP52, the FK1 domain of FKBP51 exhibits microsecond–millisecond conformational dynamics in the β3 bulge and the β4–β5 loop, known sites of protein signalling interactions. Swapping residue 119 yields altered conformational dynamics in a pattern reminiscent of reported modulations in steroid receptor activity.

scholarly journals Antibodies to Steroid Receptor Deoxyribonucleic Acid Binding Domains and their Reactivity with the Human Glucocorticoid Receptor

1988 ◽  
Vol 2 (11) ◽  
pp. 1018-1026 ◽  
Author(s):  
Elizabeth M. Wilson ◽  
Dennis B. Lubahn ◽  
Frank S. French ◽  
Christine M. Jewell ◽  
John A. Cidlowski
Keyword(s):  
Glucocorticoid Receptor ◽  
Deoxyribonucleic Acid ◽  
Steroid Receptor ◽  
Binding Domains

scholarly journals Dynamics and Selective Remodeling of the DNA Binding Domains of RPA

2018 ◽  
Author(s):  
Nilisha Pokhrel ◽  
Colleen C. Caldwell ◽  
Elliot I. Corless ◽  
Emma A. Tillison ◽  
Joseph Tibbs ◽  
...  
Keyword(s):  
Dna Binding ◽  
Conformational Dynamics ◽  
Protein A ◽  
Interacting Proteins ◽  
Ssdna Binding ◽  
Dna Binding Domains ◽  
Binding Domains ◽  
Mediator Protein ◽  
Damage Response ◽  
The Individual

AbstractReplication protein A (RPA) coordinates important DNA metabolic events by stabilizing single-strand DNA (ssDNA) intermediates, activating the DNA damage response, and handing off ssDNA to appropriate downstream players. Six DNA binding domains (DBDs) in RPA promote high affinity binding to ssDNA, but also allow RPA displacement by lower affinity proteins. We have made fluorescent versions of RPA and visualized the conformational dynamics of individual DBDs in the context of the full-length protein. We show that both DBD-A and DBD-D rapidly bind to and dissociate from ssDNA, while RPA as a whole remains bound to ssDNA. The recombination mediator protein Rad52 selectively modulates the dynamics of DBD-D. This demonstrates how RPA interacting proteins, with lower ssDNA binding affinity, can access the occluded ssDNA and remodel individual DBDs to replace RPA.One Sentence SummaryThe choreography of binding and rearrangement of the individual domains of RPA during homologous recombination is revealed.

scholarly journals Regulation of Nuclear Receptor Activity by a Pseudouridine Synthase through Posttranscriptional Modification of Steroid Receptor RNA Activator

2004 ◽  
Vol 15 (4) ◽  
pp. 549-558 ◽  
Author(s):  
Xiansi Zhao ◽  
Jeffrey R. Patton ◽  
Shannon L. Davis ◽  
Brian Florence ◽  
Sarah J. Ames ◽  
...  
Keyword(s):  
Nuclear Receptor ◽  
Steroid Receptor ◽  
Receptor Activity ◽  
Posttranscriptional Modification ◽  
Pseudouridine Synthase

BAG-1 diversely affects steroid receptor activity

2011 ◽  
Vol 441 (1) ◽  
pp. 297-303 ◽  
Author(s):  
Regina T. Knapp ◽  
Andrea Steiner ◽  
Ulrike Schmidt ◽  
Kathrin Hafner ◽  
Florian Holsboer ◽  
...  
Keyword(s):  
Androgen Receptor ◽  
Heat Shock ◽  
Heat Shock Protein 70 ◽  
Mineralocorticoid Receptor ◽  
Transcriptional Activity ◽  
Steroid Receptors ◽  
Steroid Receptor ◽  
Receptor Activity ◽  
High Homology ◽  
Shed Light

Part of the cellular and physiological functions of BAG-1 (Bcl-2-associated athanogene 1) has been ascribed to the ability of this hsp70 (heat-shock protein 70) co-chaperone to regulate steroid receptor activity. BAG-1 has been reported to inhibit the GR (glucocorticoid receptor) and stimulate the androgen receptor, but to leave the activity of the MR (mineralocorticoid receptor) unchanged. Given the high homology between the MR and GR, this disparity in the actions of BAG-1 is surprising. In the present study, we analysed the effect of BAG-1 on the activity of the closely related PR (progesterone receptor). Similarly to the GR, the transcriptional activity of the PR is inhibited by the long and middle isoforms of BAG-1, BAG-1L and BAG-1M, but not by the short isoform, BAG-1S. We found this inhibition to require the hsp70-binding domain of BAG-1. To shed light on the mechanisms that could explain BAG-1's differential actions on steroid receptors, we tested the binding of BAG-1M to the PR. Mutational analyses of the PR and BAG-1M revealed that the mode of interaction and BAG-1M-mediated inhibition of the PR differs from the reported scenario for the GR. Surprisingly, we also found binding of BAG-1M to the MR. In addition, BAG-1M was able to inhibit the transcriptional activity of the MR. These data entail a reappraisal of the physiological actions of BAG-1M on steroid receptor activity.

Reappraisal of the Role of Heat Shock Proteins as Regulators of Steroid Receptor Activity

1998 ◽  
Vol 33 (6) ◽  
pp. 437-466 ◽  
Author(s):  
T. Ylikomi ◽  
J.-M. Wurtz ◽  
H. Syvälä ◽  
S. Passinen ◽  
A. Pekki ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Steroid Receptor ◽  
Receptor Activity ◽  
Shock Proteins
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