A molecular phylogeny of wild and cultivated Echinochloa in East Asia inferred from non-coding region sequences of trnT-L-F

The phylogenetic relationship among 30 accessions belonging to nine species of the genus Echinochloa Beauv. was studied on the basis of the sequence of three non-coding regions ( trn T-L, trn L-F intergenic spacers, and trn L intron) of chloroplast DNA (cpDNA). A strict consensus parsimonious tree of the three most parsimonious trees derived from 25 polymorphic sites (six indels and 19 substitutions) in the total sequences, ranging from 1715–1760 bp, represented five groups: (i) Echinochloa oryzicola Vasing. and Echinochloa stagnina Beauv. from Thailand; (ii) Echinochloa crus-galli Beauv. complex; (iii) Echinochloa crus-pavonis Schult; (iv) Echinochloa colonum Link. and Echinochloa frumentacea Link.; and (v) the African species, Echinochloa obtusiflora Stapf and Echinochloa stagnina . Japanese barnyard millet ( Echinochloa esculenta H. Scholz) and various weedy varieties of E. crus-galli and Echinochloa oryzoides Fritsch had quite similar sequences and formed the E. crus-galli complex, which was characterized by six substitutions. A cultivated form of E. oryzicola (Mosuo barnyard millet) and various morphological and agronomical forms of E. oryzicola were characterized by two indels. Indian barnyard millet ( E. frumentacea ) and its wild counterpart ( E. colonum ) were characterized by five substitutions. Domestication as millets and adaptation to paddy environments as mimic weeds might occur after the divergence of species in the Asian Echinochloa .     

Purification and characterization of a nucleoplasmin-like protein from carp (Cyprinus carpio) eggs

ABSTRACT: Nucleoplasmin, first isolated from Xenopus laevis eggs, promotes nucleosome assembly. Hereby, we have purified a nucleoplasmin-like protein from carp ( Cyprinus carpio ) eggs using ion exchange and subsequent gel filtration columns. The protein was recognized by a polyclonal antiserum against Xenopus laevis nucleoplasmin and had an amino acid composition similar to other member of the nucleoplasmin family proteins. Partial amino acid sequences from the cyanogen bromide (CNBr)-cleaved fragments showed high homology with Xenopus nucleoplasmin. The protein was also found to form an oligomeric complex and to be phosphorylated. Moreover, this protein promoted sperm nuclear decondensation as well as that of nucleoplasmin from Xenopus laevis eggs. These results suggest that the fish protein isolated here is a member of nucleoplasmin family.