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Results: 5

1.
Figure 2

Figure 2. Randomization of the primary sequence of CTD region 1. From: Chromatin Condensing Functions of the Linker Histone C-terminal Domain are mediated by Specific Amino Acid Composition and Intrinsic Protein Disorder.

A) Schematic diagrams of wild type H1°, H1°RanS1#1, and H1°RanS1#2. B) Sedimentation coefficient distributions in TEN buffer of 208–12 nucleosomal arrays (dashed line) assembled with wild type H1° (○), H1°RanS1#1 (●), or H1°RanS1#2 (□). B) G(s) plots of 208–12 chromatin fibers bound to wild type H1° (○), H1°RanS1#1 (●), or H1°RanS1#2 (□) in 0. 25 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. D) G(s) plots of 208–12 fibers bound to wild type H1° (○), H1°RanS1#1 (●), or H1°RanS1#2 (□) in 0. 45 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. E) Oligomerization as a function of MgCl2. Shown are data for 208–12 nucleosomal arrays (dashed line) and 208–12 chromatin fibers bound to wild type H1° (○), H1°RanS1#1 (●), or H1°RanS1#2 (□). All plots are representative of results seen with 3–4 different chromatin preparations.

Xu Lu, et al. Biochemistry. ;48(1):164-172.
2.
Figure 4

Figure 4. Exchanging and swapping H1° CTD regions 1 and 3. From: Chromatin Condensing Functions of the Linker Histone C-terminal Domain are mediated by Specific Amino Acid Composition and Intrinsic Protein Disorder.

A) Schematic diagrams of wild type H1°, H1°1214, H1°3214 and H1°3234. B) Sedimentation coefficient distributions in TEN buffer of 208–12 nucleosomal arrays (▪) and 208–12 chromatin fibers bound to wild type H1° (○), H1°1214 (●), H1°3214 (△), or H1°3234 (□). C) G(s) plots of 208–12 fibers bound to wild type H1° (○), H1°1214 (●), H1°3214 (△), or H1°3234 (□) in 0. 25 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. D) G(s) plots of 208–12 fibers bound to wild type H1° (○), H1°1214 (●), H1°3214 (△), or H1°3234 (□) in 0. 45 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. E) Oligomerization as a function of MgCl2. Shown are data for 208–12 nucleosomal arrays (dashed line) assembled with wild type H1° (○), H1°1214 (●), H1°3214 (△), or H1°3234 (□). All plots are representative of results seen with 3–4 different chromatin preparations.

Xu Lu, et al. Biochemistry. ;48(1):164-172.
3.
Figure 1

Figure 1. Characterization of model chromatin fibers bound to endogenous mouse somatic linker histone isoforms. From: Chromatin Condensing Functions of the Linker Histone C-terminal Domain are mediated by Specific Amino Acid Composition and Intrinsic Protein Disorder.

A) Sedimentation coefficient distributions in low salt TEN buffer of 208–12 nucleosomal arrays (dashed line) assembled with endogenous mouse H1° (○), H1S-1(●), H1S-1(□), H1S-3 (▲), and H1S-4 (▽). B) G(s) plots of 208–12 chromatin fibers bound to wild type H1° (○), H1S-1(●), H1S-1(□), H1S-3 (▲), or H1S-4 (▽) in 0. 25 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. C) G(s) plots of 208–12 fibers bound to wild type H1° (○), H1S-1(●), H1S-1(□), H1S-3 (▲), or H1S-4 (▽) in 0. 45 mM MgCl2. D) Oligomerization as a function of MgCl2. Shown are data for 208–12 nucleosomal arrays (dashed line) and 208–12 chromatin fibers bound to wild type H1° (○), H1S-1(●), H1S-1(□), H1S-3 (▲), or H1S-4 (▽). All plots are representative of results seen with 3–4 different chromatin preparations.

Xu Lu, et al. Biochemistry. ;48(1):164-172.
4.
Figure 3

Figure 3. Mutagenesis of the amino acid composition of CTD region 1. From: Chromatin Condensing Functions of the Linker Histone C-terminal Domain are mediated by Specific Amino Acid Composition and Intrinsic Protein Disorder.

A) Schematic diagrams of wild type H1°, H1°S1TD, and H1°S1S3TD. B) Sedimentation coefficient distributions in TEN buffer of 208–12 nucleosomal arrays (dashed line) assembled with wild type H1° (○), H1°S1TD (●), or H1°S1S3TD (□). B) G(s) plots of 208–12 chromatin fibers bound to wild type H1° (○), H1°S1TD (●), or H1°S1S3TD (□) in 0. 25 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. D) G(s) plots of 208–12 fibers bound to wild type H1° (○), H1 CTD “tailless” (△), H1°S1TD (●), or H1°S1S3TD (□) in 0. 45 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. E) Oligomerization as a function of MgCl2. Shown are data for 208–12 nucleosomal arrays (dashed line) and 208–12 chromatin fibers bound to wild type H1° (○), H1°S1TD (●), or H1°S1S3TD (□). All plots are representative of results seen with 3–4 different chromatin preparations.

Xu Lu, et al. Biochemistry. ;48(1):164-172.
5.
Figure 5

Figure 5. Replacement of H1° CTD region 1 with regions 2 or 4. From: Chromatin Condensing Functions of the Linker Histone C-terminal Domain are mediated by Specific Amino Acid Composition and Intrinsic Protein Disorder.

A) Schematic diagrams of wild type H1°, H1°2234, and H1°4234. B) Sedimentation coefficient distributions in low salt TEN buffer of 208–12 nucleosomal arrays (dashed line) assembled with wild type H1° (○), H1°2234 (●), or H1°4234 (□). C) Sedimentation velocity analysis. G(s) plots of 208–12 chromatin fibers bound to wild type H1° (○), H1°2234 (●), or H1°4234 (□) in 0. 25 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. D) G(s) plots of 208–12 fibers bound to wild type H1° (○), H1°2234 (●), or H1°4234 (□) in 0. 45 mM MgCl2. The G(s) plot of H1°-bound chromatin fibers in low salt (dashed line; data from panel 1A) is shown for reference. E) Oligomerization as a function of MgCl2. Shown are data for 208–12 nucleosomal arrays (dashed line) and 208–12 chromatin fibers bound to wild type H1° (○), H1°2234 (●), or H1°4234 (□). All plots are representative of results seen with 3–4 different chromatin preparations.

Xu Lu, et al. Biochemistry. ;48(1):164-172.

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