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Arsenite-induced changes in methylation of the 70,000 dalton heat shock proteins in chicken embryo fibroblasts.

Abstract：

:Methylated lysyl and arginyl residues are present in the two major heat shock proteins, hsp70A and hsp70B, of chicken embryo fibroblasts. Here, we demonstrate that this methylation can be modulated by sodium arsenite, a chemical that increases the synthesis of hsp70. In particular, in hsp70A the amount of epsilon-N-trimethyl-lysine significantly decreases and the amount of epsilon-N-dimethyl-lysine and epsilon-N-monomethyl-lysine increases, while in hsp70B, the quantity of NG-monomethyl-arginine is reduced fivefold after arsenite treatment. To determine the specificity of these changes in methylation the pool size of S-adenosyl-L-methionine (AdoMet) and the total cellular level of methylated protein was measured. After arsenite treatment, no significant change in AdoMet pool size and the level of protein methylation was observed with the exception of an apparent increase in NG-monomethyl-arginine in total cellular protein. Thus, the arsenite-induced changes in methylation of hsp70 polypeptides are not a generalized phenomenon and may reflect a modulation in the structure or function of these two polypeptides after their induced synthesis by this chemical.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wang C,Lazarides E

doi

10.1016/s0006-291x(84)80312-5

subject

Has Abstract

pub_date

1984-03-15 00:00:00

pages

735-43

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(84)80312-5

journal_volume

119

pub_type

杂志文章

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