Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Histone crosslinked

Kuykendall JR, Bogdanffy MS. 1992. Reaction kinetics ofDNA-histone crosslinking by vinyl acetate and acetaldehyde. Carcinogenesis 13 2095-100... [Pg.518]

SADP or sulfo-SADP also have been used to study the phenylalanine-methionine-arginine-phenylalanine-amide-activated sodium channel (Coscoy et al., 1998), various apolipoprotein E isoforms (Mann et al., 1995), the high-affinity phenylalkylamine Ca2+ antagonist binding protein from guinea pig (Moebius et al., 1994), the interaction of non-histone proteins with nucleosome core particles (Reeves and Nissen, 1993), and the interactions among cytochromes P-450 in the endoplasmic reticulum (Alston et al., 1991). See Chapter 28 for methods of using photoreactive heterobifunctional crosslinkers to study protein interactions. [Pg.316]

N 077 "Unperturbed Dimensions of Crosslinked Histones Evaluated Using Random-Flight Statistics and Rotational Isomeric State Theory"... [Pg.446]

Russo, E., Giancotti, V., Cosini, S., and Crane-Robinson, C. 1981. Identification of a heterologous histone complex using reversible crosslinking. Int. J. Biol. Macromol. 3 367-369. [Pg.338]

The rate of formation of cisplatin-DNA adducts was found to be independent of superhelicity [59] and appears to be unaffected by the presence of histones in nucleosomes [29] and in chromatin [77], Therefore, isolated DNA in aqueous solution appears to be a relevant model for kinetic and mechanistic studies of cellular DNA-platination. It was early checked that the cisplatin-DNA adducts were stable for a least three days at 37 °C after their formation [78], There are now a few cases reported of unstable platinum adducts (vide supra) i) monoadducts with the diazapyrenium ligand [52], ii) a cisplatin intrastrand GG chelate rearranging into a GG interstrand crosslink [63], iii) cisplatin GG interstrand diadducts, slowly rearranging into intrastrand ones [65], tv) transplatin intrastrand GNG diadducts rearranging into interstrand crosslinks (J.-M. Malinge and M. Leng, Part 3). [Pg.231]

Figure 2.12 DNA crosslinking. The deleterious properties of nitrogen mustards are explained through the illustrated interstrand linkage mechanism that makes DNA impossible to duplicate or transcribe. Intrastrand crosslinking is the basis of action for anti-cancer drugs such as c/s-platin and carbo-platin. This is intended to prevent DNA duplication and hence cancer cell division. DNA crosslinking to proteins (such as histones) uses a non-covalent DNA intercalator with two azide functional groups. Both azides are activated for covalent coupling under photo-chemical conditions so that DNA subsequently becomes covalently linked to protein. Figure 2.12 DNA crosslinking. The deleterious properties of nitrogen mustards are explained through the illustrated interstrand linkage mechanism that makes DNA impossible to duplicate or transcribe. Intrastrand crosslinking is the basis of action for anti-cancer drugs such as c/s-platin and carbo-platin. This is intended to prevent DNA duplication and hence cancer cell division. DNA crosslinking to proteins (such as histones) uses a non-covalent DNA intercalator with two azide functional groups. Both azides are activated for covalent coupling under photo-chemical conditions so that DNA subsequently becomes covalently linked to protein.
The resulting gel slice was then run in a second dimension to determine the histone proteins specifically crosslinked. [Pg.150]

In attempts to reconstitute nucleosomes on SV40 circular DNA, Cap-lan et al. (37) observed that if the histones were ADP-rihosylated prior to reconstitution assembly of nucleosomes was inhibited by as much as 80%. If nucleosomes were first allowed to assemble, then modified by ADP-ribosylation, no eflPect on stability was observed. These data led the authors to speculate that ADP-ribosylation of histones prior to nucleosome assembly might be of physiological importance. Perella and Lea (168, 169) have shown that in rat liver nuclei, polyamines cause an increase in histone Hi ADP-ribosylation and histone HI dimer synthesis, which is accompanied by a decrease in core histone ADP-ribosylation. Data such as these have led to speculation that Hi dimer formation may function in the condensation or stabilization of chromatin fibers (35, 119). The data of Lorimer et al. (124) indicate that dimer synthesis is inversely related to the nuclear activity of the poly(ADP-ribose) glycohydrolase. Thus, these authors (124) inferred that the Hl-Hl-polymer complex formation is of a transient nature. As pointed out by Purnell et al. (171), if this crosslink were to function in the stabilization of chromatin, the modified histone Hi would have... [Pg.30]


See other pages where Histone crosslinked is mentioned: [Pg.54]    [Pg.540]    [Pg.112]    [Pg.155]    [Pg.54]    [Pg.540]    [Pg.112]    [Pg.155]    [Pg.1026]    [Pg.26]    [Pg.168]    [Pg.139]    [Pg.140]    [Pg.145]    [Pg.146]    [Pg.146]    [Pg.273]    [Pg.274]    [Pg.277]    [Pg.469]    [Pg.470]    [Pg.472]    [Pg.473]    [Pg.479]    [Pg.482]    [Pg.446]    [Pg.1074]    [Pg.54]    [Pg.119]    [Pg.50]    [Pg.582]    [Pg.277]    [Pg.1358]    [Pg.379]    [Pg.730]    [Pg.757]    [Pg.114]    [Pg.41]    [Pg.146]    [Pg.67]    [Pg.161]    [Pg.140]    [Pg.171]    [Pg.336]    [Pg.150]    [Pg.388]    [Pg.415]   
See also in sourсe #XX -- [ Pg.150 ]




SEARCH



Histone

© 2024 chempedia.info