{"id":4562,"date":"2019-10-24T19:27:32","date_gmt":"2019-10-24T10:27:32","guid":{"rendered":"http:\/\/163.180.4.222\/lab\/?p=4562"},"modified":"2019-10-24T19:27:32","modified_gmt":"2019-10-24T10:27:32","slug":"histone-lactylation-links-metabolism-and-gene-regulation","status":"publish","type":"post","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=4562","title":{"rendered":"Histone lactylation links metabolism and gene regulation"},"content":{"rendered":"<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<h5>Cells regulate gene expression in part through the chemical labelling of histone proteins. Discovery of a label derived from lactate molecules reveals a way in which cells link gene expression to nutrient metabolism.<\/h5>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<div class=\"article__aside align-right hide-print\">\n<div class=\"pdf__download shrink--aside\"><\/div>\n<\/div>\n<div class=\"align-left\">\n<div class=\"article__body serif cleared\">\n<p>Cellular metabolism involves the uptake, release and biochemical interconversion of nutrients to produce energy and synthesize complex molecules. The intermediates and end products of metabolism also have essential signalling functions, modulating cell signalling and gene expression in accordance with nutritional resources<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR1\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">1<\/a><\/sup><sup>,<\/sup><sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR2\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">2<\/a><\/sup>. One way in which these metabolites signal is through the chemical modification of proteins such as histones.\u00a0<a href=\"https:\/\/www.nature.com\/articles\/s41586-019-1678-1\" data-track=\"click\" data-label=\"https:\/\/www.nature.com\/articles\/s41586-019-1678-1\" data-track-category=\"body text link\">Writing in\u00a0<i>Nature<\/i><\/a>, Zhang and colleagues<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR3\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">3<\/a><\/sup>\u00a0describe their discovery of a previously unknown histone modification, lactylation, derived from the cellular metabolite lactate.<\/p>\n<p>&nbsp;<\/p>\n<aside class=\"recommended pull pull--left sans-serif\" data-label=\"Related\"><a href=\"https:\/\/www.nature.com\/articles\/s41586-019-1678-1\" data-track=\"click\" data-track-label=\"recommended article\"><img decoding=\"async\" class=\"recommended__image\" src=\"https:\/\/media.nature.com\/w400\/magazine-assets\/d41586-019-03122-1\/d41586-019-03122-1_17291256.jpg\" \/><\/a><\/p>\n<p class=\"recommended__title serif\">Read the paper: Metabolic regulation of gene expression by histone lactylation<\/p>\n<\/aside>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<p>Histones are central components of chromatin \u2014 a complex of DNA and proteins that organizes and regulates the genome. They can be altered by cellular enzymes, which add chemical tags such as methyl, acetyl and phosphate groups; these epigenetic modifications to the genome affect processes such as gene expression and DNA replication and repair. Zhang\u00a0<i>et al.<\/i>\u00a0predicted that histones might also be altered by the addition of lactyl groups, and they began their search for lactylation by using a technique called mass spectrometry, which has enabled the identification of numerous protein modifications in the past few years<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR4\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">4<\/a><\/sup>. By looking for shifts in the masses of amino-acid residues that make up histone tails, the authors deduced the presence of a modified lysine amino-acid residue, consistent with the addition of a lactyl group. Zhang\u00a0<i>et al.<\/i>\u00a0validated this finding by comparing synthetic peptides that had been chemically modified in this way with the corresponding peptides identified in cells.<\/p>\n<p>The authors also used metabolic tracing with a form of lactate labelled with a stable isotope of carbon (<sup>13<\/sup>C<sub>3<\/sub>-lactate) to demonstrate that lactate is involved in histone lactylation. They further found that levels of lysine lactylation rose when cells were treated with increasing doses of lactate. So, histone lactylation is derived from lactate and is sensitive to lactate levels.<\/p>\n<p>Lactate is an abundant metabolite produced during glycolysis \u2014 a central metabolic process in which glucose consumed by cells is broken down to generate energy. During glycolysis, glucose is converted into two pyruvate molecules; these can be either funnelled into lactate production or transported into the cellular power generators (the mitochondria), forming the intermediate acetyl coenzyme A (acetyl-CoA) and thence entering the Krebs cycle for energy production. Lactate is produced through glycolysis in various cell types, including cancer cells and immune cells. Its production is also enhanced under certain conditions, such as hypoxia (low oxygen levels), which suppresses pyruvate entry into the Krebs cycle. Zhang and colleagues\u2019 discovery that lactate is used for histone modification is intriguing both because of the metabolite\u2019s abundance and because its production, uptake and use are all subject to dynamic regulation<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR5\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">5<\/a><\/sup>.<\/p>\n<p>&nbsp;<\/p>\n<aside class=\"recommended pull pull--left sans-serif\" data-label=\"Related\"><a href=\"https:\/\/www.nature.com\/articles\/nature22498\" data-track=\"click\" data-track-label=\"recommended article\"><img decoding=\"async\" class=\"recommended__image\" src=\"https:\/\/media.nature.com\/w400\/magazine-assets\/d41586-019-03122-1\/d41586-019-03122-1_17291254.jpg\" \/><\/a><\/p>\n<p class=\"recommended__title serif\">Local metabolites linked to memory<\/p>\n<\/aside>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<p>One substantial question that the authors aimed to address is whether lysine lactylation responds to metabolic alterations in cells. Other metabolite-derived protein modifications \u2014 such as lysine acetylation (derived from acetyl-CoA) \u2014 are metabolically sensitive<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR2\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">2<\/a><\/sup>, providing a precedent for this idea. Zhang\u00a0<i>et al.<\/i>\u00a0found that the amount of glucose available to cells grown\u00a0<i>in vitro<\/i>\u00a0dynamically regulates the lysine lactylation of histones in those cells. Furthermore, tracing of isotopically labelled glucose (<sup>13<\/sup>C<sub>6<\/sub>-glucose) showed that lysine lactylation depends on glycolysis. The authors used several perturbations to promote lactate production (including hypoxia and inhibitors of mitochondrial metabolism) and to suppress it (using inhibitors of pyruvate conversion to lactate). The cumulative data indicate that lysine lactylation is highly sensitive to lactate production through glycolysis.<\/p>\n<p>Zhang\u00a0<i>et al.<\/i>\u00a0next sought to investigate the biological functions of lactylation, selecting macrophages as their model. Macrophages are immune cells that can take on pro-inflammatory (termed M1) or anti-inflammatory (M2) characteristics; they undergo metabolic changes that correspond to these functions<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR6\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">6<\/a><\/sup>. For example, macrophages that encounter signs of bacterial infection activate inflammatory genes and upregulate glycolysis<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR6\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">6<\/a><\/sup>. Zhang\u00a0<i>et al.<\/i>\u00a0stimulated macrophages with bacteria or with the bacterial component lipopolysaccharide (LPS) to induce M1 characteristics. They found that glycolysis increased and that intracellular levels of lactate rose progressively, parallelling an increase in histone lactylation (Fig. 1a). Notably, inflammatory genes typically associated with M1 characteristics were upregulated rapidly on exposure to LPS, but did not correlate with lactate levels or lysine lactylation (Fig. 1b). Instead, the increase in lysine lactylation was slower and correlated with the upregulation of homeostatic genes (those involved in maintaining a biological steady state).<\/p>\n<p>&nbsp;<\/p>\n<figure class=\"figure\">\n<div class=\"embed intensity--high\">\n<div class=\"embed intensity--high\"><img decoding=\"async\" class=\"figure__image\" src=\"https:\/\/media.nature.com\/w800\/magazine-assets\/d41586-019-03122-1\/d41586-019-03122-1_17297230.png\" alt=\"\" data-src=\"\/\/media.nature.com\/w800\/magazine-assets\/d41586-019-03122-1\/d41586-019-03122-1_17297230.png\" \/><\/div>\n<\/div><figcaption>\n<p class=\"figure__caption sans-serif\"><span class=\"mr10\"><b>Figure 1 | A new epigenetic modification, histone lactylation.<\/b>\u00a0Zhang and colleagues<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR3\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">3<\/a><\/sup>\u00a0have discovered a chemical modification called lactylation \u2014 the addition of a lactyl (La) group to the lysine amino-acid residues in the tails of histone proteins.\u00a0<b>a<\/b>, Stimulating immune macrophage cells with lipopolysaccharide molecules (mimicking bacterial infection) increases the conversion of glucose to energy through glycolysis. This, in turn, leads to increases in intracellular levels of the molecule lactate, and to lactylation of histones at promoter DNA sequences. However, it is unclear which enzymes generate the intermediate molecule lactyl-CoA, from which La is derived, or which enzymes deposit (writers), remove (erasers) or recognize and interpret (readers) histone lactylation.\u00a0<b>b<\/b>, Zhang\u00a0<i>et al.<\/i>\u00a0report that the increase in lysine lactylation is delayed following macrophage stimulation. This delay correlates with changes in the expression of homeostatic genes involved in maintaining a biological steady state, but not with changes in inflammatory-gene expression. The authors therefore hypothesize that lactylation generates a \u2018lactate timer\u2019 to restore normal tissue function after infection.<\/span><\/p>\n<\/figcaption><\/figure>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<p>The authors went on to investigate where lysine lactylation occurred in the M1 genome, as well as how the modification altered gene expression. They found that lysine lactylation was high in gene promoter regions (which mark the start points of gene transcription), and associated positively with the levels of messenger RNA produced from those genes. The authors also compared lysine lactylation and acetylation, finding lactylation at many genes that lack acetylation \u2014 suggesting distinct roles for the two modifications. Moreover, macrophages that could not produce lactate could increase the expression of inflammatory genes in response to stimulation with LPS, but could not upregulate lysine lactylation or the associated expression of homeostatic genes at later times. These temporal dynamics led the authors to propose that a delayed \u2018lactate timer\u2019 involving histone lactylation drives the activation of genes involved in resolving infections to help re-establish tissue homeostasis (Fig. 1b).<\/p>\n<p>These findings raise questions about the biochemistry of lactylation and its broader roles in physiology and disease. In terms of biochemistry, the authors show in a cell-free system that lactyl-CoA is a lactyl-group donor for lysine lactylation. So far, however, the enzymes that produce lactyl-CoA from lactate in the cell, as well as the cellular concentrations of lactyl-CoA, are unknown. Other unresolved questions concern the way in which lysine lactylation is regulated by the enzymes that deposit, read or remove this label. In the authors\u2019 cell-free system, an acetyltransferase enzyme known as p300 can catalyse the transfer of lactyl from lactyl-CoA to histones, but whether it does this in cells has yet to be tested.<\/p>\n<p>In terms of the broader roles of this modification, lactate is generated by cells both in physiological contexts \u2014 such as in skeletal muscle during exercise \u2014 and in the context of diseases such as cancer. In addition, lactate is taken up by cells of healthy tissues and tumours to feed the Krebs cycle<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR7\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">7<\/a><\/sup>. So, as well as occurring in glycolytic cells, lactylation might also participate in communication between cells. On this note, high lactate levels in the environment around tumours are known to promote immunosuppression<sup><a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29#ref-CR8\" data-track=\"click\" data-action=\"anchor-link\" data-track-label=\"go to reference\" data-track-category=\"references\">8<\/a><\/sup>, and Zhang\u00a0<i>et al.<\/i>\u00a0found that histone lysine lactylation was greater in tumour-associated macrophages than in those from another tissue. All in all, the authors\u2019 discovery of histone lactylation provides a launch point for a deeper investigation into the roles and regulation of this modification, which links cellular metabolism to gene regulation and could have numerous implications for human health.<\/p>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<\/div>\n<p><span class=\"emphasis\">Nature<\/span>\u00a0<strong>574<\/strong>, 492-493 (2019)<\/p>\n<p>&nbsp;<\/p>\n<div class=\"emphasis\">doi: 10.1038\/d41586-019-03122-1<\/div>\n<\/div>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<p>(\uc6d0\ubb38: <a href=\"https:\/\/www.nature.com\/articles\/d41586-019-03122-1?utm_source=feedburner&amp;utm_medium=feed&amp;utm_campaign=Feed%3A+nature%2Frss%2Fcurrent+%28Nature+-+Issue%29\">\uc5ec\uae30<\/a>\ub97c \ud074\ub9ad\ud558\uc138\uc694~)<\/p>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>&nbsp; &nbsp; Cells regulate gene expression in part through the chemical labelling of histone proteins. Discovery of a label derived from lactate molecules reveals a<a href=\"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=4562\" class=\"more-link\">(more&#8230;)<\/a><\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"_monsterinsights_skip_tracking":false,"_monsterinsights_sitenote_active":false,"_monsterinsights_sitenote_note":"","_monsterinsights_sitenote_category":0,"jetpack_post_was_ever_published":false,"_jetpack_newsletter_access":"","_jetpack_dont_email_post_to_subs":false,"_jetpack_newsletter_tier_id":0,"_jetpack_memberships_contains_paywalled_content":false,"_jetpack_memberships_contains_paid_content":false,"footnotes":"","jetpack_publicize_message":"","jetpack_publicize_feature_enabled":true,"jetpack_social_post_already_shared":true,"jetpack_social_options":{"image_generator_settings":{"template":"highway","default_image_id":0,"font":"","enabled":false},"version":2}},"categories":[33,29,30],"tags":[],"class_list":["post-4562","post","type-post","status-publish","format-standard","hentry","category-do-biology","category-lets-do-science","category-recent-science-news"],"aioseo_notices":[],"jetpack_publicize_connections":[],"jetpack_featured_media_url":"","jetpack-related-posts":[{"id":2830,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=2830","url_meta":{"origin":4562,"position":0},"title":"Modification of histone proteins by serotonin in the nucleus","author":"biochemistry","date":"March 15, 2019","format":false,"excerpt":"\u00a0 \u00a0 The function of histone proteins can be modified through addition or removal of certain chemical groups. The addition of a serotonin molecule is a newly found histone modification that could influence gene expression. \u00a0 Epigenetics has been defined as the study of heritable traits that do not involve\u2026","rel":"","context":"In &quot;Let's Do Biology!&quot;","block_context":{"text":"Let's Do Biology!","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?cat=33"},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":4699,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=4699","url_meta":{"origin":4562,"position":1},"title":"Senescent cells feed on their neighbours","author":"biochemistry","date":"October 31, 2019","format":false,"excerpt":"\u00a0 Chemotherapy-treated cancer cells that enter a non-dividing state called senescence can nevertheless boost cancer growth. The finding that these cells eat neighbouring cells reveals a mechanism that enables senescent cells to persist. \u00a0 \u00a0 Multicellular life requires individual cells to cooperate in a way that benefits the organism. Cells\u2026","rel":"","context":"In &quot;Let's Do Biology!&quot;","block_context":{"text":"Let's Do Biology!","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?cat=33"},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":3931,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=3931","url_meta":{"origin":4562,"position":2},"title":"Cancer-cell death ironed out","author":"biochemistry","date":"July 27, 2019","format":false,"excerpt":"\u00a0 \u00a0 Ferroptosis is a form of cell death. The finding that cells that have certain mutations in the Hippo signalling pathway are susceptible to ferroptosis might offer a way to treat a cancer called mesothelioma. \u00a0 \u00a0 In the late twentieth century, there was a rise in a type\u2026","rel":"","context":"In &quot;Let's Do Biology!&quot;","block_context":{"text":"Let's Do Biology!","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?cat=33"},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":3495,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=3495","url_meta":{"origin":4562,"position":3},"title":"Cooperativity in synthetic gene circuits","author":"biochemistry","date":"May 10, 2019","format":false,"excerpt":"\u00a0 \u00a0 Synthetic biologists would like to be able to make gene regulatory circuits that mimic key properties of eukaryotic gene regulation. Taking a cue from multimeric transcription factor complexes, Bashor\u00a0et al.\u00a0developed synthetic transcriptional circuits that produce nonlinear behavior from cooperativity (see the Perspective by Ng and El-Samad). Their system\u2026","rel":"","context":"In &quot;Let's Do Biology!&quot;","block_context":{"text":"Let's Do Biology!","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?cat=33"},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":4191,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=4191","url_meta":{"origin":4562,"position":4},"title":"Remodeling the genome with DNA twists","author":"biochemistry","date":"October 6, 2019","format":false,"excerpt":"\u00a0 \u00a0 In complex organisms such as humans, a single genetic blueprint can give rise to a multitude of different cell types, from nerve to liver to muscle. Such cellular diversity relies on restricting which portions of genomic DNA are accessible and therefore can be read by cellular machinery. Ultimately,\u2026","rel":"","context":"In &quot;Let's Do Biology!&quot;","block_context":{"text":"Let's Do Biology!","link":"https:\/\/biochemistry.khu.ac.kr\/lab\/?cat=33"},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":4881,"url":"https:\/\/biochemistry.khu.ac.kr\/lab\/?p=4881","url_meta":{"origin":4562,"position":5},"title":"Interfacing electronic and genetic circuits","author":"biochemistry","date":"December 14, 2019","format":false,"excerpt":"\u00a0 \u00a0 Synthetic genetic circuits leverage the information processing capability of biological machinery to tackle complex sensing tasks, yet they lack many of the advantages inherent to electrical computation. 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