Abstract
| Original language | English |
|---|---|
| Title of host publication | Chromatin remodeling |
| Subtitle of host publication | methods and protocols |
| Editors | Randall H. Morse |
| Publisher | Humana Press |
| Pages | 373-387 |
| Number of pages | 15 |
| ISBN (Electronic) | 9781617794773 |
| ISBN (Print) | 9781617794766 |
| DOIs | |
| Publication status | Published - 2012 |
Publication series
| Name | Methods in Molecular Biology |
|---|---|
| Publisher | Humana Press |
| Volume | 833 |
| ISSN (Print) | 1064-3745 |
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Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4. / Bowman, Andrew; Owen-Hughes, Tom.
Chromatin remodeling: methods and protocols. ed. / Randall H. Morse. Humana Press, 2012. p. 373-387 (Methods in Molecular Biology; Vol. 833).Research output: Chapter in Book/Report/Conference proceeding › Chapter (peer-reviewed)
TY - CHAP
T1 - Sulfyhydryl-reactive site-directed cross-linking as a method for probing the tetrameric structure of histones H3 and H4
AU - Bowman, Andrew
AU - Owen-Hughes, Tom
PY - 2012
Y1 - 2012
N2 - The structural characterisation of protein-protein interactions is often challenging. Where interactions are not amenable to high-resolution approaches, alternatives providing lower resolution information are often of value. One such approach is site-directed cross-linking. Here, through the introduction of cysteine residues at strategic locations in histone proteins, we use site-directed cross-linking to monitor the association of chromatin subunits. This approach is informative for the study of both recombinant and native chromatin complexes consisting either of histone subunits alone or in association with accessory proteins, in this case histone chaperones. The approaches described may be generally applicable for monitoring the interactions of a diverse range of multi-protein complexes.
AB - The structural characterisation of protein-protein interactions is often challenging. Where interactions are not amenable to high-resolution approaches, alternatives providing lower resolution information are often of value. One such approach is site-directed cross-linking. Here, through the introduction of cysteine residues at strategic locations in histone proteins, we use site-directed cross-linking to monitor the association of chromatin subunits. This approach is informative for the study of both recombinant and native chromatin complexes consisting either of histone subunits alone or in association with accessory proteins, in this case histone chaperones. The approaches described may be generally applicable for monitoring the interactions of a diverse range of multi-protein complexes.
UR - http://www.scopus.com/inward/record.url?scp=84855905982&partnerID=8YFLogxK
U2 - 10.1007/978-1-61779-477-3_22
DO - 10.1007/978-1-61779-477-3_22
M3 - Chapter (peer-reviewed)
C2 - 22183605
AN - SCOPUS:84855905982
SN - 9781617794766
T3 - Methods in Molecular Biology
SP - 373
EP - 387
BT - Chromatin remodeling
A2 - Morse, Randall H.
PB - Humana Press
ER -