02403nas a2200217   4500008004100000245009700041210006900138260000900207300000700216490000700223520165600230653001601886653001601902653001601918653002301934653003701957653000801994100002802002700003602030856011902066       2021                        eng d00aMethylation as a key regulator of Tau aggregation and neuronal health in Alzheimer's disease0 aMethylation as a key regulator of Tau aggregation and neuronal h  cMAY   a510 v193 a<p>Neurodegenerative diseases like Alzheimer's, Parkinson's and Huntington's disease involves abnormal aggregation and accumulation of toxic proteins aggregates. Post-translational modifications (PTMs) of the causative proteins play an important role in the etiology of disease as they could either slow down or accelerate the disease progression. Alzheimer disease is associated with the aggregation and accumulation of two major protein aggregates-intracellular neurofibrillary tangles made up of microtubule-associated protein Tau and extracellular Amyloid-beta plaques. Post-translational modifications are important for the regulation of Tau`s function but an imbalance in PTMs may lead to abnormal Tau function and aggregation. Tau methylation is one of the important PTM of Tau in its physiological state. However, the methylation signature on Tau lysine changes once it acquires pathological aggregated form. Tau methylation can compete with other PTMs such as acetylation and ubiquitination. The state of PTM at these sites determines the fate of Tau protein in terms of its function and stability. The global methylation in neurons, microglia and astrocytes are involved in multiple cellular functions involving their role in epigenetic regulation of gene expression via DNA methylation. Here, we have discussed the effect of methylation on Tau function in a site-specific manner and their cross-talk with other lysine modifications. We have also elaborated the role of methylation in epigenetic aspects and neurodegenerative conditions associated with the imbalance in methylation metabolism affecting global methylation state of cells.</p>10aAggregation10aEpigenetics10amethylation10aMethyltransferases10apost-translational modifications10aTau1 aBalmik, Abhishek, Ankur1 aChinnathambi, Subashchandrabose  uhttp://library.ncl.res.in/content/methylation-key-regulator-tau-aggregation-and-neuronal-health-alzheimers-disease02479nas a2200289   4500008004100000022001400041245014000055210006900195260000900264300001200273490000700285520151800292653002001810653001601830653000801846653001601854653003201870653002401902653001401926653002201940653001201962100001601974700002901990700002402019700002402043856012202067       2021                        eng d  a0022-095700aPolycomb group methyltransferase StE(z)2 and deposition of H3K27me3 and H3K4me3 regulate the expression of tuberization genes in potato0 aPolycomb group methyltransferase StEz2 and deposition of H3K27me  cFEB   a426-4440 v723 a<p>Polycomb repressive complex (PRC) group proteins regulate various developmental processes in plants by repressing target genes via H3K27 trimethylation, and they function antagonistically with H3K4 trimethylation mediated by Trithorax group proteins. Tuberization in potato has been widely studied, but the role of histone modifications in this process is unknown. Recently, we showed that overexpression of StMSI1, a PRC2 member, alters the expression of tuberization genes in potato. As MSI1 lacks histone-modification activity, we hypothesized that this altered expression could be caused by another PRC2 member, StE(z)2, a potential H3K27 methyltransferase in potato. Here, we demonstrate that a short-day photoperiod influences StE(z)2 expression in the leaves and stolons. StE(z)2 overexpression alters plant architecture and reduces tuber yield, whereas its knockdown enhances yield. ChIP-sequencing using stolons induced by short-days indicated that several genes related to tuberization and phytohormones, such as StBEL5/11/29, StSWEET11B, StGA2OX1, and StPIN1 carry H3K4me3 or H3K27me3 marks and/or are StE(z)2 targets. Interestingly, we observed that another important tuberization gene, StSP6A, is targeted by StE(z)2 in leaves and that it has increased deposition of H3K27me3 under long-day (non-induced) conditions compared to short days. Overall, our results show that StE(z)2 and deposition of H3K27me3 and/or H3K4me3 marks might regulate the expression of key tuberization genes in potato.</p>10aChIP-sequencing10aEpigenetics10aPcG10aphotoperiod10apolycomb repressive complex10apotato tuberization10ashort-day10aSolanum tuberosum10aStE(z)21 aKumar, Amit1 aKondhare, Kirtikumar, R.1 aMalankar, Nilam, N.1 aBanerjee, Anjan, K.  uhttp://library.ncl.res.in/content/polycomb-group-methyltransferase-stez2-and-deposition-h3k27me3-and-h3k4me3-regulate