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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Taniura, H. Gerace, L. Glass, C. |
| Description | Author Affiliation: Taniura H ( Department of Cell Biology, Scripps Research Institute, La Jolla, California 92037, USA.) |
| Abstract | Interaction of chromatin with the nuclear envelope and lamina is thought to help determine higher order chromosome organization in the interphase nucleus. Previous studies have shown that nuclear lamins bind chromatin directly. Here we have localized a chromatin binding site to the carboxyl-terminal tail domains of both A- and B-type mammalian lamins, and have characterized the biochemical properties of this binding in detail. Recombinant glutathione-S-transferase fusion proteins containing the tail domains of mammalian lamins C, B1, and B2 were analyzed for their ability to associate with rat liver chromatin fragments immobilized on microtiter plate wells. We found that all three lamin tails specifically bind to chromatin with apparent KdS of 120-300 nM. By examining a series of deletion mutants, we have mapped the chromatin binding region of the lamin C tail to amino acids 396- 430, a segment immediately adjacent to the rod domain. Furthermore, by analysis of chromatin subfractions, we found that core histones constitute the principal chromatin binding component for the lamin C tail. Through cooperativity, this lamin-histone interaction could be involved in specifying the high avidity attachment of chromatin to the nuclear envelope in vivo. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 131 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1995-10-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Chromatin Metabolism Histones Lamin Type A Lamin Type B Nuclear Proteins Amino Acid Sequence Animals Binding Sites Physiology DNA-Binding Proteins Lamins Liver Ultrastructure Molecular Sequence Data Chemistry Recombinant Fusion Proteins Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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