Homo- and Heteronuclear Two-Dimensional NMR Studies of the Globular Domain of Histone H1: Full Assignment, Tertiary Structure, and Comparison with the Globular Domain of Histone H5

Biochemistry ◽  
1994 ◽  
Vol 33 (37) ◽  
pp. 11079-11086 ◽  
Author(s):  
Corinne Cerf ◽  
Guy Lippens ◽  
V. Ramakrishnan ◽  
Serge Muyldermans ◽  
Alain Segers ◽  
...  
Keyword(s):  
Tertiary Structure ◽  
Histone H1 ◽  
Globular Domain ◽  
Two Dimensional ◽  
Nmr Studies ◽  
Histone H5

Homo- and heteronuclear two-dimensional NMR studies of the globular domain of histone H1: Sequential assignment and secondary structure

Biochemistry ◽  
1993 ◽  
Vol 32 (42) ◽  
pp. 11345-11351 ◽  
Author(s):  
Corinne Cerf ◽  
Guy Lippens ◽  
Serge Muyldermans ◽  
Alain Segers ◽  
V. Ramakrishnan ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Histone H1 ◽  
Sequential Assignment ◽  
Globular Domain ◽  
Two Dimensional ◽  
Nmr Studies

scholarly journals Precise elimination of the N-terminal domain of histone H1

1982 ◽  
Vol 203 (3) ◽  
pp. 577-582 ◽  
Author(s):  
L Böhm ◽  
P Sautière ◽  
P D Cary ◽  
C Crane-Robinson
Keyword(s):  
Tertiary Structure ◽  
Submaxillary Gland ◽  
Spectroscopic Characterization ◽  
Histone H1 ◽  
Globular Domain ◽  
Edman Degradation ◽  
Terminal Domain ◽  
C Terminus ◽  
Mouse Submaxillary Gland ◽  
Calf Thymus

The proteinase from mouse submaxillary gland was used to cleave total calf thymus histone H1 between residues 32 and 33. The C-terminal peptide, comprising residues 33 to the C-terminus, was purified and identified by amino acids analysis and Edman degradation. Spectroscopic characterization by n.m.r. for tertiary structure and by c.d. for secondary structure shows the globular domain of the parent histone H1 to be preserved intact in the peptide. It has therefore lost only the N-terminal domain and is a fragment of histone H1 comprising the globular plus C-terminal domains only. Precise elimination of only the N-terminal domain makes the fragment suitable for testing domain function in histone H1.

scholarly journals Phylogeny-Based Systematization of Arabidopsis Proteins with Histone H1 Globular Domain

2017 ◽  
Vol 174 (1) ◽  
pp. 27-34 ◽  
Author(s):  
Maciej Kotliński ◽  
Lukasz Knizewski ◽  
Anna Muszewska ◽  
Kinga Rutowicz ◽  
Maciej Lirski ◽  
...  
Keyword(s):  
Histone H1 ◽  
Globular Domain ◽  
Arabidopsis Proteins

scholarly journals Does high-mobility-group non-histone protein HMG 1 interact specifically with histone H1 subfractions?

1979 ◽  
Vol 183 (3) ◽  
pp. 657-662 ◽  
Author(s):  
P D Cary ◽  
K V Shooter ◽  
G H Goodwin ◽  
E W Johns ◽  
J Y Olayemi ◽  
...  
Keyword(s):  
Specific Interaction ◽  
High Mobility ◽  
Histone H1 ◽  
High Mobility Group ◽  
Chromosomal Protein ◽  
Histone Protein ◽  
Total Histone ◽  
Equilibrium Sedimentation ◽  
Histone H5

The interaction of the non-histone chromosomal protein HMG (high-mobility group) 1 with histone H1 subfractions was investigated by equilibrium sedimentation and n.m.r. sectroscopy. In contrast with a previous report [Smerdon & Isenberg (1976) Biochemistry 15, 4242–4247], it was found, by using equilibrium-sedimentation analysis, that protein HMG 1 binds to all three histone H1 subfractions CTL1, CTL2, and CTL3, arguing against there being a specific interaction between protein HMG 1 and only two of the subfractions, CTL1 and CTL2. Raising the ionic strength of the solutions prevents binding of protein HMG 1 to total histone H1 and the three subfractions, suggesting that the binding in vitro is simply a non-specific ionic interaction between acidic regions of the non-histone protein and the basic regions of the histone. Protein HMG 1 binds to histone H5 also, supporting this view. The above conclusions are supported by n.m.r. studies of protein HMG 1/histone H1 subfraction mixtures. When the two proteins were mixed, there was little perturbation of the n.m.r. spectra and there was no evidence for specific interaction of protein HMG 1 with any of the subfractions. It therefore remains an open question as to whether protein HMG 1 and histone H1 are complexed together in chromatin.

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