Dynamic properties of independent chromatin domains measured by correlation spectroscopy in living cells

Table 2 Dynamic and structural parameters of histone-FP-labeled chromatin domains obtained with FCS at different nuclear localizations

		n	Loop-rosette, blob; theta-solvent conditions^a			Loop-rosette; good-solvent conditions^b			Globular^b
		n	τ ₁ (ms)	R _g (nm)	gc (Mb)	τ ₁ (ms)	R _g (nm)	gc (Mb)	R _g (nm)	gc (Mb)
H1-EGFP untreated	Perinuclear	35	91 ± 6	245 ± 5	0.80–1.12	100 ± 6	289 ± 6	1.31–1.83	240 ± 5	0.75–1.05
	Perinucleolar	34	78 ± 6	234 ± 6	0.70–0.98	94 ± 5	283 ± 5	1.23–1.73	235 ± 4	0.71–0.99
	Euchromatin	62	161 ± 15	297 ± 9	0.83–1.16	191 ± 20	359 ± 12	1.47–2.05	298 ± 10	0.84–1.17
H2A-EGFP untreated	Perinucle(ol)ar	84	83 ± 7	238 ± 4	0.73–1.03	90 ± 8	279 ± 4	1.18–1.65	232 ± 4	0.68–0.95
H2A-EGFP untreated	Euchromatin	84	165 ± 11	299 ± 9	0.85–1.19	188 ± 14	356 ± 13	1.43–2.00	297 ± 11	0.83–1.16
H2B-mCherry untreated	Perinucle(ol)ar	84	94 ± 6	249 ± 4	0.84–1.18	102 ± 7	291 ± 4	1.34–1.88	242 ± 3	0.77–1.08
H2B-mCherry untreated	Euchromatin	84	174 ± 10	304 ± 9	0.89–1.25	195 ± 12	361 ± 12	1.49–2.09	300 ± 10	0.86–1.12
H1-EGFP TSA-treated	Perinucle(ol)ar	25	292 ± 34	362 ± 14	1.65–2.31	366 ± 49	445 ± 20	3.07–4.30	370 ± 17	1.77–2.47
H1-EGFP TSA-treated	Nucleoplasm	18	307 ± 37	368 ± 15	1.74–2.43	384 ± 51	453 ± 20	3.24–4.54	377 ± 17	1.87–2.61
H1-EGFP ATP-depleted	Perinucle(ol)ar	17	303 ± 51	367 ± 21	1.72–2.41	388 ± 74	454 ± 29	3.26–4.57	378 ± 24	1.88–2.64
H1-EGFP ATP-depleted	Nucleoplasm	25	278 ± 43	356 ± 18	1.57–2.20	351 ± 59	439 ± 25	2.95–4.13	365 ± 21	1.69–2.37

(mean value ± standard error; min. value–max. value)
τ ₁—decay time of the first polymer relaxation mode, R _g—radius of gyration of topologically and dynamically independent chromatin domain, gc—genomic content of topologically and dynamically independent chromatin domain
^aRelaxation times and radii of gyration are numerically identical for loop-rosette conformation under theta-solvent conditions and for blob conformation
^bRelaxation times are numerically identical for loop-rosette conformation under good-solvent conditions and for globular conformation

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