至今,GenScript的服务及产品已被Cell, Nature, Science, PNAS等1300多家生物医药类杂志引用近万次,处于行业领先水平。NIH、哈佛、耶鲁、斯坦福、普林斯顿、杜克大学等约400家全球著名机构使用GenScript的基因合成、多肽服务、抗体服务和蛋白服务等成功地发表科研成果,再次证明GenScript 有能力帮助业内科学家Make research easy.

Ubinuclein-1 confers histone H3 3-specific-binding by the HIRA histone chaperone complex

Nature Communications . 2015; 
M Daniel Ricketts, Brian Frederick, Henry Hoff, Yong Tang, David C. Schultz, Taranjit Singh Rai, Maria Grazia Vizioli, Peter D. Adams & Ronen Marmorstein
Products/Services Used Details Operation
Biochemicals Large scale peptide synthesis of UBN1(122–148) and FITC-UBN1(127–148) was commissioned by a commercial vendor (Genscript). Get A Quote

摘要

Histone chaperones bind specific histones to mediate their storage, eviction or deposition from/or into chromatin. The HIRA histone chaperone complex, composed of HIRA, ubinuclein-1 (UBN1) and CABIN1, cooperates with the histone chaperone ASF1a to mediate H3.3-specific binding and chromatin deposition. Here we demonstrate that the conserved UBN1 Hpc2-related domain (HRD) is a novel H3.3-specific-binding domain. Biochemical and biophysical studies show the UBN1-HRD preferentially binds H3.3/H4 over H3.1/H4. X-ray crystallographic and mutational studies reveal that conserved residues within the UBN1-HRD and H3.3 G90 as key determinants of UBN1–H3.3-binding specificity. Comparison of the structure with the unrel... More

关键词