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. 2016 Feb 24;5(3):372–380. doi: 10.1242/bio.016733

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© 2016. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Fig. 3. — Quantitative analysis of FRAP recovery of domain switch constructs. (A) Sequence alignment of H1.1 and H1.5. The sequence span representing the globular domain is marked with a black bar. Arrows represent the location of the complimentary Sac1 and Hind3 restriction sites used to swap domains between the two variants. (B) Schematic of domain switch mutants. Construct 551 consists of residues 1-99 of H1.5 and residues 102-213 of H1.1; Construct 115 consists of residues 1-101 of H1.1 and residues 100-223 of H1.5. Construct 511 consists of residues 1-42 of H1.5 and residues 45-213 of H1.1. Construct 155 consists of residues 1-44 of H1.1 and residues 43-223 of H1.5. Construct 151 consists of residues 1-44 of H1.1, residues 43-99 of H1.5 and residues 102-213 of H11. Construct 515 consists of residues 1-42 of H1.5, residues 45-101 of H1.1 and residues 100-223 of H1.5. (C-E) Quantitative analysis of FRAP recovery of cells expressing the indicated domain switch constructs as GFP fusions. (F) Plotted t₅₀ values represent means±s.d. from at least 12 cells (see Table 2).