By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Proteins are discussed in a new report. According to news reporting originating in Cambridge, United Kingdom, by NewsRx journalists, research stated, "Proteins of the ankyrin-repeat and SOCS-box (ASB) family act as the substrate-recognition subunits of ECS-type (ElonginBC-Cullin-SOCS-box) Cullin RING E3 ubiquitin ligase (CRL) complexes that catalyze the specific polyubiquitination of cellular proteins to target them for degradation by the proteasome. Therefore, ASB multimeric complexes are involved in numerous cell processes and pathways; however, their interactions, assembly, and biological roles remain poorly understood."
The news reporters obtained a quote from the research from the University of Cambridge, "To enhance our understanding of ASB CRL systems, we investigated the structure, affinity, and assembly of the quaternary multisubunit complex formed by ASB9, Elongin B, Elongin C (EloBC), and Cullin S. Here, we describe the application of several biophysical techniques including differential scanning fluorimetry, isothermal titration calorimetry (ITC), nanoelectrospray ionization, and ion-mobility mass spectrometry (IM-MS) to provide structural and thermodynamic information for a quaternary ASB CRL complex. We find that ASB9 is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 N-terminal domain (Cul5(NTD)) but not to Cul2(NTD). The structure of the monomeric ASB9-EloBC-Cul5(NTD) quaternary complex is revealed by molecular modeling and is consistent with IM-MS and temperature-dependent ITC data. This is the first experimental study to validate structural information for the assembly of the quaternary N-terminal region of an ASB CRL complex. The results suggest that ASB E3 ligase complexes function and assemble in an analogous manner to that of other CRL systems and provide a platform for further molecular investigation of this important protein family."
According to the news reporters, the research concluded: "The data reported here will also be of use for the future development of chemical probes to examine the biological function and modulation of other ECS-type CRL systems."
For more information on this research see: Multimeric Complexes among Ankyrin-Repeat and SOCS-box Protein 9 (ASB9), ElonginBC, and Cullin 5: Insights into the Structure and Assembly of ECS-type Cullin-RING E3 Ubiquitin Ligases. Biochemistry, 2013;52(31):5236-5246. Biochemistry can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Biochemistry - www.pubs.acs.org/journal/bichaw)
Our news correspondents report that additional information may be obtained by contacting J.C. Thomas, University of Cambridge, Dept. of Chem, Cambridge CB2 1EW, United Kingdom. Additional authors for this research include D. Matak-Vinkovic, I. Van Molle and A. Ciulli (see also Proteins).
Keywords for this news article include: Europe, Ligases, Proteins, Cambridge, Ubiquitins, United Kingdom, Enzymes and Coenzymes
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