RESUMO
Objective@#The purpose of this study was to determine the effect of climbing exercise intervention on gross motor function in children aged 8 to 9 years, and to provide a theoretical basis and scientific reference for the application of climbing exercise in the improvement of children health.@*Methods@#Random sampling method was used to select 53 children aged 8-9 from a public school in Haidian District in Beijing, and children were randomly divided into control group (n=30) and exercise group (n=23), children in the exercise group received climbing exercises for 8 weeks . KTK test was used to assess gross motor development.@*Results@#After intervention, the gross motor level of male and female children in Exercise group were significantly higher than before (in male group, before intervention, KTK score：217.5±32.3，after intervention, KTK score：245.1±24.2，P<0.01；in female group, before intervention, KTK score: 219.6±30.3, after intervention, KTK score: 246.9±23.2，P<0.01); while the gross motor level in control group had no significant change compared to the intervention state before(in male group, before intervention, KTK score：219.9±26.8，after intervention, KTK score：224.8±30.2，P>0.05；in female group, before intervention, KTK score: 216.6±18.1，after intervention, KTK score:214.8±28.6，P>0.05). There were no differences of gross motor level between sham and exercise group at baseline (P>0.05). After intervention, except the MS scores (P>0.05), other test program scores were higher than those of control group (in exercise group, WB: 52.1±6.8; HH: 61.7±8.7; JS: 73.7±7.6; in control group, WB: 43.1±9.9; HH: 54.5±15.2; JS: 64.9±6.8) (P<0.01).@*Conclusion@#Our research shows that climbing exercise intervention helps promoting the children’s physical quality, and establishes substantial foundation for the formation and promotion of sports cognition and complex motor skills.
RESUMO
We report here that PHO2 protein is also phosphorylated by an unidentified protein kinase. A Ser-230 to Ala mutation in the consensus sequence (SPIK) recognized by cc2/CDC28-related kinase in the PHO2 protein led to the complete loss of its ability to activate the transcription of PHO5 gene. Further work showed that Pro-231 to Ser mutation inactivated PHO2 protein as well, while Ser-230 to Asp mutation did not affect PHO2 activity. Since PHO2 Asp-230 mutant mimics Ser-230 phosphorylated PHO2, we postulate that only phosphorylated PHO2 protein could activate the transcription of the PHO5 gene. The results of in vitro phospho-labelling experiments showed that the whole cell extract of the YPH499 strain grown under low phosphate conditions phosphorylated GST (glutathione S-transferase)- PHO2 (wild type) fusion protein, but not the GST-PHO2 mutant (Pro-231 to Ser) protein in which the putative phosphorylation sequence was destroyed. We therefore propose that the PHO2 protein may also be phosphorylated in vitro at Ser-230, and the phosphorylation of this site may be necessary for its function in controlling PHO5 gene expression.
