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Interaction of polyadenylic acid (5′) with histone H1 or protamine
Author(s) -
Kuo WuNan,
Chambers Maxine C.,
JnBaptiste Junior B.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201852
Subject(s) - protamine , histone h1 , histone , histone h2a , histone octamer , chemistry , biochemistry , microbiology and biotechnology , histone methyltransferase , biology , dna , nucleosome , heparin
The interaction between polyadenylic acid (5′) (poly[A]) and histone (or protamine) was analyzed by electrophoretic retardation of poly[A]‐histone (or protamine) complex in agarose gel. The potency of interaction was protamine > histone H1, arginine‐rich histone > other histones. The catalytic subunit of cyclic AMP‐dependent protein kinase effectively decreased the electrophoretic retardation of poly[A]‐histone H1. The interaction between poly[A] and histone H1 was also detected by the drastically enhanced absorbance around 340 nm. The findings may implicate a regulatory role of histone H1 on mRNAs through its binding on poly[A] tails.