Open AccessA major nucleolar protein, nucleolin, induces chromatin decondensation by binding to histone Hl
Author(s) -
ERARD Monique S.,
BELENGUER P.,
CAIZERGUESFERRER M.,
PANTALONI A.,
AMALRIC F.
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb14224.x
Subject(s) - nucleolin , histone octamer , chromatin , histone h1 , nucleosome , microbiology and biotechnology , histone h2a , histone , histone code , chemistry , biology , biochemistry , dna , nucleolus , cytoplasm
Using circular dichroism to probe the extent of DNA condensation in chromatin, we have demonstrated that a major nucleolar protein, nucleolin, can decondense chromatin. By means of various binding assays we show that nucleolin has a strong affinity for histone H1 and that the phosphorylated N‐terminal domain, rich in lengthy stretches of acidic amino acids, is responsible for this ionic interaction. Additional experiments clearly demonstrate that nucleolin is unable to act as a nucleosome core assembly or disassembly factor and hence has little affinity for the core histone octamer. We propose that this nucleolar protein induces chromatin decondensation by binding to histone H1, and that nucleolin can therefore be regarded as a protein of the high‐mobility‐group type.