| FEBS Letters | |
| Metaphase‐specific* phosphorylations weaken the association between chromosomal proteins HMG 14 and 17, and DNA | |
| Lund, Terje2  Berg, Kristian1  | |
| [1] Norwegian Radium Hospital, Institute of Cancer Research, Department of Biophysics, Montebello, Oslo, Norway;Department of Biochemistry, University of Oslo, Norway | |
| 关键词: Metaphase; Phosphorylation; High-mobility-group proteins; DNA affinity; | |
| DOI : 10.1016/0014-5793(91)80921-O | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
The high-mobility-group proteins HMG 14 and 17 have been isolated from human cells arrested in metaphase. The affinity between an unphosphorylated and two phosphorylated forms of these proteins, and DNA has been investigated using columns of single-stranded and double-stranded DNA. It was shown that the most phosphorylated forms had much lower affinity for single-stranded and double-stranded DNA compared to the unphosphorylated form present in interphase cells. The results are in accordance with the view that HMG 14 and 17 may dissociate transiently from chromatin during mitosis.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020295294ZK.pdf | 447KB |
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