Cofractionation of HMGB proteins with histone dimers.
Anal Biochem
; 447: 98-106, 2014 Feb 15.
Article
in En
| MEDLINE
| ID: mdl-24239809
ABSTRACT
An effective and flexible method is presented that can be used to investigate cofractionation of groups of nuclear proteins. The method was used to analyze chromatin-related proteins, of which high-mobility group B (HMGB) proteins consistently cofractionated by cation-exchange chromatography with the histone dimer (H2A-H2B). This led to the hypothesis that the two form a complex, further suggested by gel filtration, in which the HMGBs with core histones eluted as a defined high-molecular-weight peak. A necessary requirement for further studying protein interactions is that the constituents are of the highest possible purity and the pure histone dimers and tetramers used in this study were derived from pure histone octamers with their native marks. There is a growing interest in protein-protein interactions and an increasing focus on protein-interaction domains most frequently, pull-down assays are used to examine these. The technology presented here can provide an effective system that complements pull-down assays.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Histones
/
HMGB Proteins
/
Protein Multimerization
/
Chemical Fractionation
Limits:
Animals
Language:
En
Journal:
Anal Biochem
Year:
2014
Type:
Article
Affiliation country:
United kingdom