Interaction of polyadenylic acid (5') with histone H1 or protamine.
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.
Kuo
W N
WN
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114-3099, USA.
Chambers
M C
MC
Jn-Baptiste
B
B
D002147:Calmodulin / Q000494:pharmacology; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D004587:Electrophoresis, Agar Gel; D006657:Histones / Q000737:chemistry* / Q000302:isolation & purification; D046911:Macromolecular Substances; D011061:Poly A / Q000737:chemistry* / Q000302:isolation & purification; D011479:Protamines / Q000737:chemistry* / Q000302:isolation & purification; D011485:Protein Binding; D013056:Spectrophotometry, Ultraviolet
D002147:Calmodulin; D006657:Histones; D046911:Macromolecular Substances; D011479:Protamines; D011061:Poly A; D017868:Cyclic AMP-Dependent Protein Kinases