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Nucleoside triphosphate binding and hydrolysis by histone H1.

Abstract：

:We present here further evidence supporting that histone H1 contains a nucleotide binding site interacting e.g. with ADP, ATP, GDP and GTP. The finding is in accordance with the previous observation that nucleotides modulate recognition of DNA by H1. Most interestingly, H1 appears to be capable of hydrolyzing NTPs and incorporating phosphate to exogenous proteins. The mode of nucleotide action on H1 may be considered highly analogous to that of GTPases. Nuclear receptors may thus act through mechanisms similar to those for receptors on the plasma membrane.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Mannermaa RM,Oikarinen J

doi

10.1016/s0006-291x(05)80146-9

subject

Has Abstract

pub_date

1992-01-15 00:00:00

pages

309-17

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)80146-9

journal_volume

182

pub_type

杂志文章

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