![](/images/graphics-bg.png)
Thermal and Chemical Stability of Two Homologous POZBTB Domains of KCTD Proteins Characterized by a Different Oligomeric Organization
Joint Authors
Pirone, Luciano
Esposito, Carla
Correale, Stefania
Graziano, Giuseppe
Di Gaetano, Sonia
Vitagliano, Luigi
Pedone, Emilia
Source
Issue
Vol. 2013, Issue 2013 (31 Dec. 2013), pp.1-8, 8 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2013-11-06
Country of Publication
Egypt
No. of Pages
8
Main Subjects
Abstract EN
POZ/BTB domains are widespread modules detected in a variety of different biological contexts.
Here, we report a biophysical characterization of the POZ/BTB of KCTD6, a protein that is involved in the turnover of the muscle small ankyrin-1 isoform 5 and, in combination with KCTD11, in the ubiquitination and degradation of HDAC1.
The analyses show that the domain is a tetramer made up by subunits with the expected α/β structure.
A detailed investigation of its stability, carried out in comparison with the homologous pentameric POZ/BTB domain isolated from KCTD5, highlights a number of interesting features, which are shared by the two domains despite their different organization.
Their thermal/chemical denaturation curves are characterized by a single and sharp inflection point, suggesting that the denaturation of the two domains is a cooperative two-state process.
Furthermore, both domains present a significant content of secondary structure in their denatured state and a reversible denaturation process.
We suggest that the ability of these domains to fold and unfold reversibly, a property that is somewhat unexpected for these oligomeric assemblies, may have important implications for their biological function.
Indeed, these properties likely favor the formation of heteromeric associations that may be essential for the intricate regulation of the processes in which these proteins are involved.
American Psychological Association (APA)
Pirone, Luciano& Esposito, Carla& Correale, Stefania& Graziano, Giuseppe& Di Gaetano, Sonia& Vitagliano, Luigi…[et al.]. 2013. Thermal and Chemical Stability of Two Homologous POZBTB Domains of KCTD Proteins Characterized by a Different Oligomeric Organization. BioMed Research International،Vol. 2013, no. 2013, pp.1-8.
https://search.emarefa.net/detail/BIM-1003577
Modern Language Association (MLA)
Pirone, Luciano…[et al.]. Thermal and Chemical Stability of Two Homologous POZBTB Domains of KCTD Proteins Characterized by a Different Oligomeric Organization. BioMed Research International No. 2013 (2013), pp.1-8.
https://search.emarefa.net/detail/BIM-1003577
American Medical Association (AMA)
Pirone, Luciano& Esposito, Carla& Correale, Stefania& Graziano, Giuseppe& Di Gaetano, Sonia& Vitagliano, Luigi…[et al.]. Thermal and Chemical Stability of Two Homologous POZBTB Domains of KCTD Proteins Characterized by a Different Oligomeric Organization. BioMed Research International. 2013. Vol. 2013, no. 2013, pp.1-8.
https://search.emarefa.net/detail/BIM-1003577
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1003577