Interaction of polyadenylic acid (5′) with histone H1 or protamine

Abstract

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.

Determination of nitric oxide in hydrophytes using poly(methacrylic acid-ethylene glycol dimethacrylate) monolith microextraction coupled to high-performance liquid chromatography with fluorescence detection

“…It has been reported that NO was of ubiquitous occurrence in higher plants, including foliage, intact seeds, individual seed components and in roots [38][39][40]. The interplay between NO and ethylene in the regulation of maturation and senescence of plant tissue has been already evidenced [41].…”

The Role of Nitric Oxide in Plants

“…NOS-like activity has been reported to be present in plant chloroplasts and peroxysomes (3,50). Mouse anti-NOS antibodies recognized NOS, or a NOS-like molecule, in peas, wheat, and corn (35,51,55). Ninneman and Maier (48) observed notable levels citrulline formation in higher plants, and also demonstrated NOS activity in plants by employing inhibitors such as L-NNA (NG-nitro-L-arginine) and L-NAME (NW-nitro-L-arginine methyl ester).…”