EVALUATION OF FIVE SUGAR CANE PLANTERS

Brazil is the world biggest producer of sugar cane with an area of 7x10(6) hectares. Mainly the system used for planting is the semi-mechanized one, which consists in opening the furrows with a machine, manually allocating the fractioned stalks and then covering the furrows done by the machines. The great amount of human labor used in the semi-mechanized system is becoming harder to find and also more expensive, indicating the need of a fully mechanized operation. Currently in Brazil these agriculture machines industries offers six different types of fully mechanized sugar cane planters (two types of whole stalks for planting and four using mechanized harvested stalks known as billets). All of them plant in two furrows simultaneously in 1.5 m row spacing. This study analyzed five different machines and the following variables: Working Speed (km h(-1)); Effective Capacity (ha h(-1)), Drawbar Force (kgf), Draw Bar Power (in HP), Fuel Consumption (L h(-1)) and Costs (US$ ha(-1)) comparing them with the semi-mechanized system. This research also characterized the stalks for planting as viable gems number (%), non viable gems number (%) and billet length (m). And lastly the mechanized planting system is cheaper than the conventional one and none of the machines has an adequate mechanism for placing the right amount of sugar cane seed.

Myosin Va phosphorylated on ser(1650) is found in nuclear speckles and redistributes to nucleoli upon inhibition of transcription

Nuclear actin and nuclear myosins have been implicated in the regulation of geneexpression in vertebrate cells. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. In this study, myosin-Va, phosphorylated on a conserved serine in the tail domain (phospho-ser(1650) MVa), was localized to subnuclear compartments. A monoclonal antibody, 9E6, raised against a peptide corresponding to phosphoserine(1650) and flanking regions of the murine myosin Va sequence, was immunoreactive to myosin Va heavy chain in cellular and nuclear extracts of HeLa cells, PC12 cells and B16-F10 melanocytes. Immunofluorescence microscopy with this antibody revealed discrete irregular spots within the nucleoplasm that colocalized with SC35, a splicing factor that earmarks nuclear speckles. Phospho-ser(1650) MVa was not detected in other nuclear compartments, such as condensed chromatin, Cajal bodies, gems and perinucleolar caps. Although nucleoli also were not labeled by 9E6 under normal conditions, inhibition of transcription in HeLa cells by actinomycin D caused the redistribution of phospho-ser(1650) MVa to nucleoli, as well as separating a fraction of phosphoser(1650) MVa from SC35 into near-neighboring particles. These observations indicate a novel role for myosin Va in nuclear compartmentalization and offer a new lead towards the understanding of actomyosin-based gene regulation.