The interaction of high mobility proteins HMG14 and 17 with nucleosomes
- 1 January 1980
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 8 (17) , 3757-3778
- https://doi.org/10.1093/nar/8.17.3757
Abstract
The interaction of the high mobility group proteins, HMG14 and HMG17, with nucleosome core particles has been studied. The results show that two molecules of HMG14/17 can be bound tightly but reversibly to each core particle and that their affinity for core particles is greater than their affinity for histone-free DNA of core size. Thermal denaturation and nuclease digestion studies suggest that major sites of interaction are located near the ends of the nucleosome core DNA. When nucleosome preparations from chicken erythrocyte nuclei stripped of HMG proteins are partially titrated with HMG14/17, the nucleosome-HMG complex fraction is enriched in beta-globin gene sequences.Keywords
This publication has 23 references indexed in Scilit:
- The primary structure of non‐histone chromosomal protien HMG17 from chicken erythrocyte nucleiFEBS Letters, 1980
- Hb switching in chickensCell, 1980
- Interaction of HMG 14 and 17 with actively transcribed genesCell, 1980
- Chromatin fractionation procedure that yields nucleosomes containing near-stoichiometric amounts of high mobility group nonhistone chromosomal proteinsBiochemistry, 1979
- The primary structure of the nucleosome‐associated chromosomal protein HMG 14FEBS Letters, 1979
- Structure of the chromatosome, a chromatin particle containing 160 base pairs of DNA and all the histonesBiochemistry, 1978
- Kinetic analysis of deoxyribonuclease I cleavages in the nucleosome core: Evidence for a DNA superhelixJournal of Molecular Biology, 1978
- The Primary Structure of a Non-histone Chromosomal ProteinEuropean Journal of Biochemistry, 1977
- Pancreatic DNAase cleavage sites in nucleiCell, 1977
- Mapping DNAase I-susceptible sites in nucleosomes labeled at the 5′ endsCell, 1976