Publication in refereed journal
香港中文大学研究人员 ( 现职)
| 韦妙宜教授 (那打素护理学院) |
全文
| 数位物件识别号 (DOI) http://dx.doi.org/10.1006/jmbi.1997.1235 |
引用次数
Web of Sciencehttp://aims.cuhk.edu.hk/converis/portal/Publication/279WOS source URL
其它资讯
摘要The four core histone proteins, H2A, H2B, H3, and H4 of Xenopus laevis have been individually expressed in milligram quantities in Escherichia coli. The full-length proteins and the ''trypsin-resistant'' globular domains were purified under denaturing conditions and folded into histone octamers. Both intact and truncated recombinant octamers, as well as chicken erythrocyte octamer, were assembled into nucleosome core particles using a 146 bp defined-sequence DNA fragment from a 5 S RNA gene. The three types of core particles were characterized and compared by gel electrophoresis, DNase I cleavage, and tyrosine fluorescence emission during stepwise dissociation with increasing ionic strength. Nucleosome core particles containing native and mutant histones made in bacteria have facilitated its X-ray structure determination at 2.8 Angstrom resolution. (C) 1997 Academic Press Limited.
着者Luger K, Rechsteiner TJ, Flaus AJ, Waye MMY, Richmond TJ
期刊名称JOURNAL OF MOLECULAR BIOLOGY
出版年份1997
月份9
日期26
卷号272
期次3
出版社ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
页次301 - 311
国际标準期刊号0022-2836
电子国际标準期刊号1089-8638
语言英式英语
关键词chromatin; histone; nucleosome care particle; protein expression; recombinant nucleosome
Web of Science 学科类别Biochemistry & Molecular Biology; BIOCHEMISTRY & MOLECULAR BIOLOGY
