The H3 bivalent modifications of trimethylationat Lys9 and acetylation at Lys18(H3-K9 Me3-K18 Ac) were identified to collectively recruit TRIM33 in the nodal signaling pathway.To understand the underlying mechanism of...The H3 bivalent modifications of trimethylationat Lys9 and acetylation at Lys18(H3-K9 Me3-K18 Ac) were identified to collectively recruit TRIM33 in the nodal signaling pathway.To understand the underlying mechanism of TRIM33 recruitment,the nucleosome core particles(NCPs) containing full-length H3-K9 Me3-K18 Ac were indispensable samples.Herein we developed a pseudo dipeptide strategy to efficiently prepare peptide segments,facilitating the chemical synthesis of H3-K9 Me3-K18 Ac at a tens of milligram scale.The synthetic H3-K9 Me3-K18 Ac was then examined by CD spectroscopy,which demonstrated a prominent shift compared to recombinant H3.Finally,bivalently modified NCPs were assembled and verified by gel mobility shift assay with good homogeneity.展开更多
Dear Editor, Accurate measurement of distances within and between biological macromolecules is important for structure-function studies, for investigating conformational changes and dynamics, and for improving restrai...Dear Editor, Accurate measurement of distances within and between biological macromolecules is important for structure-function studies, for investigating conformational changes and dynamics, and for improving restraints for molecular dynamics and modeling programs （Hellmich and Glaubitz, 2009）. Several methods have been developed to measure the distances between atoms, residues, and domains in single proteins and larger complexes. Fluorescence reso- nance energy transfer （FRET） is currently the most fre- quently used method to derive distances in cells or protein complexes, but the bulky size of the fluorescence probes and the strict requirement for frequency profile overlap between the acceptor and donor chromophores are limita- tions in many cases （Prevo and Peterman, 2014）.展开更多
基金supported by the National Natural Science Foundation of China(Nos.21708036,31470740,U1732161)Anhui Provincial Natural Science Foundation (No.1808085QC63)。
文摘The H3 bivalent modifications of trimethylationat Lys9 and acetylation at Lys18(H3-K9 Me3-K18 Ac) were identified to collectively recruit TRIM33 in the nodal signaling pathway.To understand the underlying mechanism of TRIM33 recruitment,the nucleosome core particles(NCPs) containing full-length H3-K9 Me3-K18 Ac were indispensable samples.Herein we developed a pseudo dipeptide strategy to efficiently prepare peptide segments,facilitating the chemical synthesis of H3-K9 Me3-K18 Ac at a tens of milligram scale.The synthetic H3-K9 Me3-K18 Ac was then examined by CD spectroscopy,which demonstrated a prominent shift compared to recombinant H3.Finally,bivalently modified NCPs were assembled and verified by gel mobility shift assay with good homogeneity.
文摘Dear Editor, Accurate measurement of distances within and between biological macromolecules is important for structure-function studies, for investigating conformational changes and dynamics, and for improving restraints for molecular dynamics and modeling programs （Hellmich and Glaubitz, 2009）. Several methods have been developed to measure the distances between atoms, residues, and domains in single proteins and larger complexes. Fluorescence reso- nance energy transfer （FRET） is currently the most fre- quently used method to derive distances in cells or protein complexes, but the bulky size of the fluorescence probes and the strict requirement for frequency profile overlap between the acceptor and donor chromophores are limita- tions in many cases （Prevo and Peterman, 2014）.
