A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones - PubMed (original) (raw)

A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones

H Taniura et al. J Cell Biol. 1995 Oct.

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.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Biochemistry. 1990 Oct 16;29(41):9551-60 - PubMed
    1. J Mol Biol. 1989 Aug 5;208(3):405-15 - PubMed
    1. Curr Opin Cell Biol. 1991 Feb;3(1):82-6 - PubMed
    1. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
    1. Curr Opin Cell Biol. 1994 Feb;6(1):25-33 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources