»Staatenverantwortlichkeit für Völkermord«

Petrossian, Gurgen

doi:10.3790/978-3-428-55628-1

Cited by 7 publications

(2 citation statements)

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“…The other structural class of KMTs are the seven-β-strand proteins, which contain an alternating seven strand β-sheet with a C-terminal β-hairpin stacked between α-helices within their catalytic domain [40,48,59]. In yeast, the enzymes Dot1, Rkm5, and Efm2 through Efm7 are members of this class (Figure 1; Table 1).…”

Section: Budding Yeast Lysine Methyltransferasesmentioning

confidence: 99%

“…Due to limitations in current approaches and only a small number of conditions tested, this list of methylated proteins is almost certainly incomplete. Additionally, there are candidate KMTs for which no substrates have yet been identified [9,14,49,73] and most KMTs have only been linked to a single substrate (see Table 1), although it is expected that a number of these enzymes will target more than one substrate. The primary methods that have been applied to identifying lysine methylated proteins in yeast have been mass spectrometry-based approaches that rely on variations of heavy methyl stable isotope labeling of amino acids in cell culture (SILAC) and analyses of whole cell lysates or fractionated lysates [9,67,73].…”

Section: Assays In Yeastmentioning

confidence: 99%

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Using Yeast to Define the Regulatory Role of Protein Lysine Methylation

Jethmalani

Green

2020

CPPS

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: The post-translational modification (PTM) of proteins are crucial for cells to survive under diverse environmental conditions and to respond to stimuli. PTMS are known to govern a broad array of cellular processes including signal transduction and chromatin regulation. The PTM lysine methylation has been extensively studied within the context of chromatin and the epigenetic regulation of the genome. However, it has also emerged as a critical regulator of non-histone proteins important for signal transduction pathways. While the number of known non-histone protein methylation events is increasing, the molecular functions of many of these modifications are not yet known. Proteomic studies of the model system Saccharomyces cerevisiae suggest lysine methylation may regulate a diversity of pathways including transcription, RNA processing, translation, and signal transduction cascades. However, there has still been relatively little investigation of lysine methylation as a broad cellular regulator beyond chromatin and transcription. Here, we outline our current state of understanding of non-histone protein methylation in yeast and propose ways in which the yeast system can be leveraged to develop a much more complete picture of molecular mechanisms through which lysine methylation regulates cellular functions.

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Section: Budding Yeast Lysine Methyltransferasesmentioning

confidence: 99%