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Kinetics of chemical modification of arginine and lysine residues in calf thymus histone H1
Author(s) -
Mita Kazuei,
Ichimura Sachiko,
Zama Mitsuo,
Hamana Koei
Publication year - 1981
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1981.360200602
Subject(s) - lysine , chemistry , arginine , residue (chemistry) , chemical modification , guanidine , histone h1 , molecule , stereochemistry , kinetics , solvent , biochemistry , histone , organic chemistry , amino acid , physics , quantum mechanics , gene
The arginine and lysine residues of calf thymus histone H1 were modified with large molar excesses of 2,3‐butanedione and O ‐methylisourea, respectively. Kinetic study of the modification reaction of the arginine residue revealed that the reaction is divided into the two pseudo‐first‐order processes. About a third (1 Arg) of the total arginine residues of the H1 molecule was rapidly modified without causing any detectable structural change of the molecule, and the slow modification of the remaining arginine residues (2 Arg) led to a loss of the folded structure of H1. In the case of lysine residue modification, 93% (56 Lys) of the total lysine residues of the H1 was modified with the same rate constant, while 7% (4 Lys) of lysine residue remained unmodified. When the reaction was performed in the presence of 6 M guanidine‐HCl, all of lysine residues were modified. It is concluded that the 2 arginine and 4 lysine residues resistant to modification are buried in interior regions of the H1 molecule and play an important role in the formation of the H1 globular structure, while the other 1 arginine and 56 lysine residues are exposed to solvent.