This experiment was conducted to breed a very early maturing variety of Italian ryegrass (Lolium multiflorum Lam.) in Grassland and Forage Crops Division, National Institute of Animal Science, RDA, Cheonan 2015-2017. The new variety of Italian ryegrass, ‘Green call 2ho’ is a diploid variety with green in leaf color and has semi-erect growth habit in late autumn and erect growth habit in early spring, ‘Green call 2ho’ was in heading date as a early-maturing variety April 24. Also ‘Green call 2ho’ was narrower by 2 mm in flag leaf width, longer by 2.5 cm in flag leaf length and shorter by 3 cm in plant height than those of the control variety, ‘Florida 80’, respectively. ‘Green call 2ho’ was also thicker by 0.33 mm in stem thickness and strong in winter hardness. Dry matter (DM) yield (11,688 kg/ha) of ‘Green call 2ho’ was 7% higher than that of ‘Florida 80’. Total digestible nutrient (TDN), crude protein (CP) and relative feed value (RFV) of ‘Green call 2ho’ were 61.3 %, 9.8 % and 98.2, respectively which are 2.6, 0.6, and 8.4 % higher, respectively than those of ‘Florida 80’, respectively. Acid detergent fiber (ADF) and neutral detergent fiber (NDF) of ‘Green call 2ho’ were 34.9 and 58.5 % which are 3.3 and 2.7 % lower than those of ‘Florida 80’, respectively.
Acute lymphoblastic leukemia (ALL), a predominantly pediatric disease involving uncontrolled proliferation of white blood cells within the bone marrow, is strongly associated with chromosomal translocations. The human chromosomal translocation t(12;21)(p12;q22) is the most frequently encountered chromosomal rearrangement in pediatric B-lineage ALL, and results in fusion of the TEL and RUNX1 genes. The resulting TEL/RUNX1 fusion protein is generally thought to be a transcriptional repressor that interferes with RUNX1-mediated transactivation. We used a luciferase assay system to investigate the effects of TEL/RUNX1 and PEBP2β on RUNX1-mediated transactivation. TEL/RUNX1 blocked the synergistic transactivation achieved by PEBP2β and RUNX1, and coimmunoprecipitation and immunofluorescence analyses showed that PEBP2β interacted with TEL/RUNX1 and was sequestered in the cytoplasm. Theses results suggest that TEL/RUNX1 inhibits RUNX1-mediated transactivtion via cytoplasmic sequestration of coactivator(s) such as PEBP2β.