Movement and Physiological Demands of Australasian National Rugby League Referees.

Purpose: To evaluate the movement and physiological demands of the Australasian National Rugby League (NRL) referees, officiating with a ‘two referee’ (i.e., ‘lead’ and ‘pocket’) system and to compare the demands of the lead referee and pocket referees. Methods: 10 Hz global positioning system devices were used to obtain 86 data sets (‘lead’, n=41; ‘pocket’, n=45) on 19 NRL referees. Total distance, relative distance covered and heart rate per half and across match-play was examined within and between referees using t-tests. Distance, time and number of movement 'efforts' were examined in six velocity classifications (i.e., standing 7.0 m.s-1) using ANOVA. Cohen's d effect sizes were reported. Results: There were no significant differences between the ‘lead’ and ‘pocket’ referee for any movement or physiological variable. There was an overall significant (large; very large) effect for distance (% distance) and time (% time) (P 5.51 m.s-1. Conclusions: Findings highlight the intermittent nature of rugby league refereeing, but show that there were no differences in the movement and physiological demands of the two refereeing roles. Findings are valuable for those responsible for the preparation, training and conditioning of NRL referees, and to ensure training prepares for and simulates match demands

UCS protein function is partially restored in the Saccharomyces cerevisiae she4 mutant with expression of the human UNC45-GC, but not UNC45-SM

A dedicated UNC45, Cro1, She4 (UCS) domain-containing protein assists in the Hsp90-mediated folding of the myosin head. Only weak sequence conservation exists between the single UCS protein of simple eukaryotes (She4 in budding yeast) and the two UCS proteins of higher organisms (the general cell and striated muscle UNC45s; UNC45-GC and UNC45-SM, respectively). In vertebrates, UNC45-GC facilitates cytoskeletal functions, whereas the 55% identical UNC45-SM assists assembly of the contractile apparatus of cardiac and skeletal muscles. A Saccharomyces cerevisiae she4Δ mutant, totally lacking any UCS protein, was engineered to express as its sole Hsp90 either the Hsp90α or the Hsp90β isoforms of human cytosolic Hsp90. A transient induction of the human UNC45-GC, but not UNC45-SM, could rescue the defective endocytosis in these she4Δ cells at 39 °C, irrespective of whether they possessed Hsp90α or Hsp90β. UNC45-GC-mediated rescue of the localisation of a Myo5-green fluorescent protein (GFP) fusion to cortical patches at 39 °C was more efficient in the yeast containing Hsp90α, though this may relate to more efficient functioning of Hsp90α as compared to Hsp90β in these strains. Furthermore, inducible expression of UNC45-GC, but not UNC45-SM, could partially rescue survival at a more extreme temperature (45 °C) that normally causes she4Δ mutant yeast cells to lyse. The results indicate that UCS protein function has been most conserved-yeast to man-in the UNC45-GC, not UNC45-SM. This may reflect UNC45-GC being the vertebrate UCS protein that assists formation of the actomyosin complexes needed for cytokinesis, cell morphological change, and organelle trafficking-events also facilitated by the myosins in yeast