TY - JOUR
T1 - Conversion of Cysteine into Dehydroalanine Enables Access to Synthetic Histones Bearing Diverse Post-Translational Modifications
AU - Chalker, Justin
AU - Lercher, Lukas
AU - Rose, Nathan
AU - Schofield, Christopher
AU - Davis, Benjamin
PY - 2012/2/20
Y1 - 2012/2/20
N2 - Six for the price of one: From a single precursor, dehydroalanine, six distinct post-translational modifications can be site-selectively installed on histone proteins (see figure), including the first site-selective phosphorylation and glycosylation of histones. Direct observation of histone deacetylase activity on a full-length modified histone as well as its interactions with both chromatin reader and writer/eraser proteins are reported.
AB - Six for the price of one: From a single precursor, dehydroalanine, six distinct post-translational modifications can be site-selectively installed on histone proteins (see figure), including the first site-selective phosphorylation and glycosylation of histones. Direct observation of histone deacetylase activity on a full-length modified histone as well as its interactions with both chromatin reader and writer/eraser proteins are reported.
KW - chromatin
KW - enzymes
KW - histone
KW - phosphorylation
KW - protein modifications
KW - synthetic biology
UR - http://www.scopus.com/inward/record.url?scp=84856887479&partnerID=8YFLogxK
U2 - 10.1002/anie.201106432
DO - 10.1002/anie.201106432
M3 - Article
SN - 1433-7851
VL - 51
SP - 1835
EP - 1839
JO - Angewandte Chemie-International Edition
JF - Angewandte Chemie-International Edition
IS - 8
ER -