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Phosphorylation and chromatin mechanics: the central importance of substrate conformation in determining the patterns of HL-60 nuclear phosphorylation.

Abstract：

:HL-60 nuclear autophosphorylation was studied in vitro under circumstances in which the conformation of chromatin was manipulated with both polyamines and DNAse-I. A general re-arrangement of the phosphorylation patterns occurred as polyamines were removed and nuclei were observed to expand. DNAse-I treatment reduced these phosphorylation patterns to a much simpler configuration indicating that the responding substrates were DNA-associated. It was concluded that substrate conformation was the main determining factor in the control of nuclear protein phosphorylation. These results suggest a method of general utility for the identification of truly nuclear proteins by the characteristics of their phosphate acceptor activity.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Testori A,Skinner JD,Murray AW,Burgoyne LA

doi

10.1016/s0006-291x(05)81296-3

subject

Has Abstract

pub_date

1991-10-15 00:00:00

pages

329-33

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)81296-3

journal_volume

180

pub_type

杂志文章

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