Mind-body practices (MBP) are known to induce electrophysiological and morphological changes, whereas reports related to changes of neurotrophins are surprisingly scarce. Consequently, in the current paper, we focused on the Quadrato motor training (QMT), a newly developed whole-body movement-based MBP, which has been reported to enhance creativity. Here we report the effects of 4 weeks of daily QMT on creativity and proNGF level in two interrelated studies. In Study A, we examined the effects of QMT compared with a walking training (WT) in healthy adults, utilizing the alternate uses task. In contrast with the WT, QMT resulted in increased creativity. In addition, the change in creativity negatively correlated with the change in proNGF levels. In Study B, we examined QMT effects on creativity and additional metacognitive functions in children, using a nonintervention group as control. Similar to Study A, following QMT, we found a negative correlation of proNGF with creativity, as well as working memory updating and planning ability. Together, the current results point to the relationship between increased creativity and decreased proNGF following MBP. Thus, the current research emphasizes the importance of widening the scope of examination of “MBP in motion” in relation to metacognition and well-being.
Using whole-brain structural measures coupled to analysis of salivary brain-derived neurotrophic factor (BDNF), we demonstrate sensory motor training-induced plasticity, including cerebellar gray matter volume increment and increased BDNF level. The increase of cerebellar volume was positively correlated with the increase of BDNF level.
We have defined the in vivo heterochromatin structure of the left telomere of Saccharomyces cerevisiae chromosome III (LIII). Analysis of heterochromatin of a single telomere was so far lacking, due to the difficulties intrinsic to the highly repetitive nature of telomeric sequences. In LIII, the terminal (C 1-3 A) n repetitive sequences are followed by a complete X element and by the single copy Ty5-1 retrotransposon. Both the telosome and the X element exhibit overall resistance to micrococcal nuclease digestion reflecting their tight chromatin structure organization. The X element contains protein complexes and irregularly distributed but well localized nucleosomes. In contrast, a regular array of phased nucleosomes is associated with the promoter region of Ty5-1 and with the more centromere-proximal sequences. The lack of a structural component of yeast telomeres, the SIR3 protein, does not alter the overall tight organization of the X element but causes a nucleosome rearrangement within the promoter region of Ty5-1 and releases Ty5-1 silencing. Thus, Sir3p links the modification of the heterochromatin structure with loss of transcriptional silencing.Telomeres play an essential role in cell biology in stabilizing chromosomes and facilitating complete replication of chromosomal termini. Telomeric DNA usually contains tandem repetitions of a short motif flanked by subtelomeric middle repetitive sequences (1). In yeast, telomeric sequences are composed of about 350 base pairs containing the (C 1-3 A) n repeats and are followed by two main subtelomeric sequences: the YЈ and X elements (2). Y elements are highly conserved and are found in about 70% of the telomeres (2-5). X elements are present in all telomeres and can exist in two main forms: a complete form containing the X core and the STR-A,B,C,D (6) elements or a short form containing essentially the X core or part of it (2, 4 -6). The complete X is found in about 80% of the telomeres, whereas uncomplete forms are found in the remaining 20%.Previous reports have referred to the chromatin structure of yeast telomeres as heterochromatin. This denomination is based on structural and functional similarities that yeast telomeres share with Drosophila heterochromatin (7-9). In Saccharomyces cerevisiae the terminal (C 1-3 A) n repeats are organized into a nuclease-resistant structure called telosome (10, 11) that does not contain nucleosomes and is associated with the protein RAP1 (10 -13). This protein binds to the repetitive (C 1-3 A) n sequences (14, 15) and interacts with other proteins including RIF1, RIF2, SIR3,. The proteins SIR3 and SIR4 interact with each other, RAP1, and the amino terminus of the histones H3 and H4. Thus, the building of the telomeric heterochromatic structures in yeast involves complex homotypic and heterotypic interactions.Although the chromatin structure of yeast telomeres is probably the best known among all eukaryotes, its specific organization is still poorly understood. It is known that both YЈ and X elements contain nucleosomes (1...
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