Comparative transcriptome analysis reveals molecular regulators underlying pluripotent cell induction and callus formation in Anthurium andraeanum “Alabama”

In Vitro Cellular & Developmental Biology - Plant - Shoot regeneration from pluripotent cell masses is an important process for genetic improvement of Anthurium andraeanum through...     

A genome-wide survey of microRNA truncation and 3′ nucleotide addition events in larch (Larix leptolepis)

MicroRNAs (miRNAs) play essential roles in numerous developmental and metabolic processes in animals and plants. Although the framework of miRNA biogenesis and function is established, the mechanism of miRNA degradation or modification remains to be investigated in plants. Mature miRNAs may be truncated or added nucleotides to generate variants. A detailed analysis of small RNA deep sequencing data sets resulted in the cloning of a large number of variants derived from larch miRNAs. Many 5′- and/or 3′-end truncated versions of miRNAs suggested that larch miRNAs might be degraded through either 5′–3′ or 3′–5′. The relative abundance of variants truncated from 3′-end was higher than that of 5′-end for most miRNAs. The addition of adenine, uridine, and cytidine to the 3′-end of miRNAs was globally present, and the subtle variability in isomiR abundance might be regulated and biologically meaningful. It is the first report for cytidine addition in plant, and our examination of published small RNA deep sequencing data sets of Arabidopsis, rice, and moss suggests that cytidine addition to miRNA 3′-end exists broadly in plants. In addition, the nucleotide addition might be associated with 3′–5′ miRNA degradation. Our results provide valuable information for a genome-wide survey of miRNA truncation and modification in larch or plants.     

Protein purification by chemo‐selective precipitation using thermoresponsive polymers

A recoverable and thermoresponsive polymer‐protein bioconjugate is synthesized and employed in the purification of protein with free sulfhydryl groups. Initiator with disulphide was modified on the cysteine residue of the target protein. Poly(N‐isopropylacrylamide) exhibiting a lower critical solution temperature was grown from the protein. The resulting protein–polymer conjugate was successfully thermoprecipitated and separated from other proteins. The approach was demonstrated with bovine serum albumin with the recycling yield of 76.4%. Enzyme activity test with papain verified the reversible polymer modification protected protein under extreme environments without affecting the functionality of the protein. This study implies the favorable potential of chemo‐selective enriching and purification of proteins.