منابع مشابه
Histones with High Lysine Content
1. The preparation and properties of lysine-rich histones, which differ in a number of respects from the classical arginine-rich histones, have been described. 2. Lysine-rich histones, like those previously known, are located in cell nuclei. 3. Lysine-rich histones dissociate more readily from combination with nucleic acid than do other histones.
متن کاملLysine methylation: beyond histones.
Posttranslational modifications (PTMs) of histone proteins, such as acetylation, methylation, phosphorylation, and ubiquitylation, play essential roles in regulating chromatin dynamics. Combinations of different modifications on the histone proteins, termed 'histone code' in many cases, extend the information potential of the genetic code by regulating DNA at the epigenetic level. Many PTMs occ...
متن کاملHistones with High L¥sine Content by M. M. Daly and A. E. Mirsky
This paper deals with some basic proteins of cell nuclei which differ in a number of ways from the classical histones of Kossel. Two characteristics of a histone noted by Kossel are its high arginine content and its way of being precipitated on addition of an excess of ammonium hydroxide (1-2). A high arginine content would tend to give a protein a basic isoelectric point and precipitability in...
متن کاملSpecies and organ specificity in very lysine-rich histones.
Very lysine-rich histones were extracted by aqueous trichloracetic acid from calf thymus, from the thymus, mammary gland, and liver of rabbits, and from chicken livers. The elution profiles of these histones, obtained by chromatography on Amberlite IRC-50 with a shallow guanidinium chloride gradient, revealed that the very lysine-rich histone complement varied from one animal species to another...
متن کاملLysine methyltransferase SETD6 modifies histones and non-histone proteins
Although central to regulating the access to genetic information, most lysine methyltransferases remain poorly characterised relative to other family of enzymes. Herein, we report new substrates for the lysine methyltransferase SETD6. Based on the SETD6catalysed site on the histone variant H2AZ, we identified similar sequences in the canonical histones H2A, H3, and H4 that are modified by SETD6...
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ژورنال
عنوان ژورنال: Journal of General Physiology
سال: 1955
ISSN: 1540-7748,0022-1295
DOI: 10.1085/jgp.38.3.405