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文章數：97 |
 茶六燒肉堂團體宴客合適嗎？》公益路美食推薦｜吃貨實測十間真心話 |
| 創作｜散文 2026/04/22 07:10:40 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
身為一個熱愛美食、喜歡在城市裡挖掘驚喜的人，臺中公益路一直是我最常出沒的地方之一。這條路可說是「臺中人的美食戰場」，從精緻西餐到創意火鍋，從日式丼飯到義式早午餐，每走幾步，就會有完全不同的特色料理餐廳。 這次我特別花了一整個月，實際造訪了公益路上十間口碑不錯的餐廳。有的是網友熱推的打卡名店，也有隱藏在巷弄裡的小驚喜。我以環境氛圍、口味表現、價格CP值與再訪意願為基準，整理出這篇實測評比。希望能幫正在猶豫去哪裡吃飯的你，找到那一間「吃完會想再來」的餐廳。 評比標準與整理方向
這次我走訪的10家餐廳橫跨不同料理類型，從高質感牛排館到巷弄系早午餐，每一間都有自己獨特的風格。為了讓整體比較更客觀，我依照以下四大面向進行評比，並搭配實際用餐體驗來打分。
整體而言，我希望這份評比不只是「哪家好吃」，而是幫你在不同情境下（約會、家庭聚餐、朋友小聚、商業午餐）都能快速找到合適的選擇。畢竟，美食不只是味覺的滿足，更是一段段與朋友共享的生活記憶。 10間臺中公益路餐廳評比懶人包公益路向來是臺中人聚餐的首選地段，從火鍋、燒肉到中式料理與早午餐，每走幾步就有驚喜。以下是我實際造訪過的10間代表性餐廳清單，橫跨平價、創意、高級各路風格。
一頭牛日式燒肉｜炭香濃郁的和牛饗宴，約會聚餐首選
走在公益路上，很難不被 一頭牛日式燒肉 的木質外觀吸引。低調卻不失質感的門面，搭配昏黃燈光與暖色調的內裝，讓人一進門就感受到濃濃的日式職人氛圍。店內空間不大，但桌距規劃得宜，每桌皆設有獨立排煙設備，烤肉時完全不怕滿身油煙味。 餐點特色
一頭牛的靈魂，絕對是他們招牌的「三國和牛拼盤」。 用餐體驗整體節奏掌握得非常好。店員會在你剛想烤下一片肉時貼心遞上夾子、幫忙換烤網，讓人完全不用分心。整場用餐過程就像一場表演，從視覺、嗅覺到味覺都被滿足。 綜合評分
地址：408臺中市南屯區公益路二段162號電話：04-23206800 小結語一頭牛日式燒肉不僅是「吃肉的地方」，更像是一場五感盛宴。從進門那一刻到最後一道甜點，都能感受到他們對細節的用心。 TANG Zhan 湯棧｜文青系火鍋代表，麻香湯底與視覺美感並重
在公益路這條美食戰線上，TANG Zhan 湯棧 是讓人一眼就會想走進去的那一種。 餐點特色
湯棧最有名的當然是它的「麻香鍋」。 用餐體驗整體氛圍比一般火鍋店更有質感。 綜合評分
地址：408臺中市南屯區公益路二段248號電話：04-22580617 官網：https://www.facebook.com/TangZhan.tw/ 小結語TANG Zhan 湯棧 把傳統火鍋做出新的樣貌保留臺式鍋物的溫度，又結合現代風格與細節服務，讓吃鍋這件事變得更有品味。 如果你想找一間兼具「好吃、好拍、好放鬆」的火鍋店，湯棧會是公益路上最有風格的選擇之一。 NINI 尼尼臺中店｜明亮寬敞的義式早午餐天堂
如果說前兩間是肉食愛好者的天堂，那 NINI 尼尼臺中店 絕對是想放鬆、聊聊天的好地方。餐廳外觀以白色系與大片玻璃窗為主，陽光灑進室內，讓人一踏入就有種度假般的輕盈感。假日早午餐時段特別熱鬧，建議提早訂位。 餐點特色
NINI 的菜單融合義式與臺灣人口味，選擇多樣且份量十足。主打的 松露燉飯 濃郁卻不膩口，米芯保留微Q口感；而 香蒜海鮮義大利麵 則以新鮮白蝦、花枝與淡菜搭配微辣蒜香，口感層次豐富。 用餐體驗店內氣氛輕鬆不拘謹，無論是一個人帶電腦工作、或朋友聚餐，都能找到舒服角落。餐點上桌速度穩定，服務人員態度親切、補水與收盤都非常主動。整體節奏讓人覺得「時間變慢了」，很適合想遠離忙碌日常的人。 綜合評分
地址：40861臺中市南屯區公益路二段18號電話：04-23288498 小結語NINI 尼尼臺中店是一間能讓人放下手機、慢慢吃飯的餐廳。餐點不追求浮誇，而是以「剛剛好」的份量與風味，陪伴每個平凡午後。如果你在找一間能邊吃邊聊天、拍照也漂亮的早午餐店，NINI 會是你在公益路上最不費力的幸福選擇。 加分100%浜中特選昆布鍋物｜平價卻用心的湯頭系火鍋，家庭聚餐好選擇
在公益路這條高質感餐廳林立的戰場上，加分100%浜中特選昆布鍋物 走的是截然不同的路線。它沒有浮誇的裝潢、也沒有高價位的套餐，但靠著實在的湯頭與親切的服務，默默吸引許多回頭客。每到用餐時間，總能看到家庭或情侶三兩成群地圍著鍋邊聊天。 餐點特色
主打 北海道浜中昆布湯底，湯頭清澈卻不單薄，越煮越能喝出海藻與柴魚的自然香氣。 用餐體驗整體氛圍偏家庭取向，桌距寬敞、座位舒適，帶小孩來也不覺擁擠。店員態度親切，補湯、收盤都很勤快，給人一種「被照顧著」的安心感。 綜合評分
地址：403臺中市西區公益路288號電話：0910855180 小結語加分100%浜中特選昆布鍋物是一間「不浮誇、但會讓人想再訪」的火鍋店。它不追求豪華擺盤，而是用最簡單的湯頭與新鮮食材，傳遞出家常卻不平凡的溫度。 印月餐廳｜中式料理的藝術演繹，宴客與家庭聚會首選
說到臺中公益路的中式料理代表，印月餐廳 絕對是榜上有名。這間開業多年的餐廳以「中菜西吃」的概念聞名，把傳統中式料理以現代手法重新詮釋。從建築外觀到餐具擺設，每個細節都散發著低調的典雅氣息。 餐點特色
印月最令人印象深刻的是他們將傳統中菜融入創意手法。 用餐體驗服務方面完全對得起餐廳的高級定位。從入座、點餐到上菜節奏，都拿捏得恰如其分。每道菜都會有服務人員細心介紹食材與吃法，讓人感受到「被款待」的尊榮感。 綜合評分
地址：408臺中市南屯區公益路二段818號電話：0422511155 小結語印月餐廳是一間「不只吃飯，更像品味生活」的地方。 KoDō 和牛燒肉｜極致職人精神，專為儀式感與頂級味覺而生
若要形容 KoDō 和牛燒肉 的用餐體驗，一句話足以總結——「像在欣賞一場關於肉的表演」。 餐點特色
這裡主打 日本A5和牛冷藏肉，以「精切厚燒」的方式呈現。 用餐體驗KoDō 的最大特色是「儀式感」。 綜合評分
地址：403臺中市西區公益路260號電話：0423220312 官網：https://www.facebook.com/kodo2018/ 小結語KoDō 和牛燒肉不是日常餐廳，而是一場體驗。 永心鳳茶｜在茶香裡用餐的優雅時光，臺味早午餐的新詮釋
走進 永心鳳茶公益店，彷彿進入一間有氣質的茶館。 餐點特色
永心鳳茶的餐點結合中式靈魂與西式擺盤，無論是「炸雞腿飯」還是「紅玉紅茶拿鐵」，都能讓人感受到熟悉卻不平凡的味道。 用餐體驗店內服務人員態度溫和，對茶品介紹詳盡。上餐節奏剛好，不急不徐。 綜合評分
地址：40360臺中市西區公益路68號三樓(勤美誠品)電話：0423221118 小結語永心鳳茶讓人重新定義「臺味」。 三希樓｜老饕級江浙功夫菜，穩重又帶人情味的中式饗宴
位於公益路上的 三希樓 是許多臺中老饕的口袋名單。 餐點特色
三希樓的菜色以 江浙與港式料理 為主，兼顧傳統與現代風味。 用餐體驗三希樓的服務給人一種老派但貼心的感覺。 綜合評分
地址：408臺中市南屯區公益路二段95號電話：0423202322 官網：https://www.sanxilou.com.tw/ 小結語三希樓是一間「吃得出功夫」的餐廳。 一笈壽司｜低調奢華的無菜單日料，職人手藝詮釋旬味極致
在熱鬧的公益路上，一笈壽司 低調得幾乎不顯眼。 餐點特色
一笈壽司採 Omakase（無菜單料理） 形式，每一餐都由主廚根據當日食材設計。 用餐體驗整場用餐約90分鐘，節奏緩慢但沉穩。 綜合評分
地址：408臺中市南屯區公益路二段25號電話：0423206368 官網：https://www.facebook.com/YIJI.sushi/ 小結語一笈壽司是一間真正讓人「放慢呼吸」的餐廳。 茶六燒肉堂｜人氣爆棚的和牛燒肉聖地，肉香與幸福感同時滿分
若要票選公益路上「最難訂位」的餐廳，茶六燒肉堂 絕對名列前茅。 餐點特色
茶六主打 和牛燒肉套餐，價格約落在 $700–$1000 間，份量與品質兼具。 用餐體驗茶六的服務效率相當高。店員親切、換網勤快、補水速度快，整場用餐流程流暢無壓力。 綜合評分
地址：403臺中市西區公益路268號電話：0423281167 官網：https://inline.app/booking/-L93VSXuz8o86ahWDRg0:inline-live-karuizawa/-LUYUEIOYwa7GCUpAFWA 小結語茶六燒肉堂用「穩定品質＋輕奢氛圍」抓住了臺中年輕族群的心。 吃完10家公益路餐廳後的心得與結語吃完這十家餐廳後，臺中公益路不只是一條美食街，而是一段生活風景線。 有的餐廳講究細膩與儀式感，像 一頭牛日式燒肉 與 一笈壽司，讓人感受到食材最純粹的美好 有的則以親切與溫度打動人心，像 加分昆布鍋物、永心鳳茶，讓人明白吃飯不只是為了飽足，而是一種被照顧的幸福。 而像茶六燒肉堂、TANG Zhan 湯棧 這類人氣名店，則用穩定的品質與熱絡的氛圍，成為許多臺中人心中「想吃肉就去那裡」的代名詞。 這十家店，構成了公益路最動人的縮影 有華麗的，也有溫柔的；有傳統的，也有創新的。 每一家都在自己的風格裡發光，讓人吃到的不只是料理，而是一種生活的溫度與節奏。 對我而言，這不僅是一場美食旅程，更是一趟關於「臺中味道」的回憶之旅。 FAQ：關於臺中公益路美食常見問題Q1：公益路哪一區的餐廳最集中？ Q2：需要提前訂位嗎？ 最後的話若要用一句話形容這趟美食之旅，我會說： 一頭牛日式燒肉飲料值得加點嗎？ 如果你也和我一樣喜歡用味蕾探索一座城市，那就把這篇公益路美食攻略收藏起來吧。NINI 尼尼臺中店調味偏重嗎？ 無論是約會、慶生、家庭聚餐，或只是想犒賞一下辛苦的自己——這條路上永遠會有一間剛剛好的餐廳在等你。三希樓有提供尾牙方案嗎？ 下一餐，不妨從這10家開始。NINI 尼尼臺中店適合辦尾牙嗎？ 打開手機、約上朋友，讓公益路成為你生活裡最容易抵達的小確幸。三希樓用餐時間會不會太短？ 如果你有私心愛店，也歡迎留言分享，加分100%浜中特選昆布鍋物CP 值高嗎？ 你的推薦，可能讓我下一趟美食旅程變得更精彩。加分100%浜中特選昆布鍋物有提供尾牙方案嗎？ Leukocytes, human white blood cells, swim using a mechanism called molecular paddling. Researchers have discovered that human leukocytes can swim using a novel mechanism called molecular paddling. Human white blood cells, known as leukocytes, swim using a newly described mechanism called molecular paddling, researchers report in the Biophysical Journal. This microswimming mechanism could explain how both immune cells and cancer cells migrate in various fluid-filled niches in the body, for good or for harm. “The capacity of living cells to move autonomously is fascinating and crucial for many biological functions, but mechanisms of cell migration remain partially understood,” says co-senior study author Olivier Theodoly of Aix-Marseille University in France. “Our findings shed new light on the migration mechanisms of amoeboid cells, which is a crucial topic in immunology and cancer research.” Cells have evolved different strategies to migrate and explore their environment. For example, sperm cells, microalgae, and bacteria can swim through shape deformations or by using a whip-like appendage called a flagellum. By contrast, somatic mammalian cells are known to migrate by attaching to surfaces and crawling. It is widely accepted that leukocytes cannot migrate on 2D surfaces without adhering to them. A prior study reported that certain human white blood cells called neutrophils could swim, but no mechanism was demonstrated. Another study showed that mouse leukocytes could be artificially provoked to swim. It is widely thought that cell swimming without a flagellum requires changes in cell shape, but the precise mechanisms underlying leukocyte migration have been debated. This is a 3D videomicroscopy of the cytoskeleton of a swimming lymphocyte showing protrusions traveling along cell body that mimic a breast-stroke motion. Credit: SoSPIM microscopy: L. Aoun, O. Theodoly, M. Biarnes, R. Galland In contrast to previous studies, Theodoly, co-senior study author Chaouqi Misbah of Grenoble Alpes University, and their collaborators provide experimental and computational evidence in the new study that human leukocytes can migrate on 2D surfaces without sticking to them and can swim using a mechanism that does not rely on changes in cell shape. “Looking at cell motion gives the illusion that cells deform their body like a swimmer,” Misbah says. “Although leukocytes display highly dynamic shapes and seem to swim with a breast-stroke mode, our quantitative analysis suggests that these movements are inefficient to propel cells.” Instead, the cells paddle using transmembrane proteins, which span the cell membrane and protrude outside the cell. The researchers show that membrane treadmilling — rearward movement of the cell surface — propels leukocyte migration in solid or liquid environments, with and without adhesion. However, the cell membrane does not move like a homogenous treadmill. Some transmembrane proteins are linked to actin microfilaments, which form part of the cytoskeleton and contract to allow cells to move. The actin cytoskeleton is widely accepted as the molecular engine propelling cell crawling. The new findings demonstrate that actin-bound transmembrane proteins paddle and propel the cell forward, whereas freely diffusing transmembrane proteins hinder swimming. This video shows imaging of the backward treadmilling of paddling molecules outside the cell. Credit: TIRF microscopy: N Garcia-Seyda Protein Recycling Drives Continuous Cellular Movement The researchers propose that continuous paddling is enabled by a combination of actin-driven external treadmilling and inner recycling of actin-bound transmembrane proteins through vesicular transport. Specifically, the paddling proteins at the rear of the cell are enclosed inside a vesicle that pinches off from the cell membrane and transported to the front of the cell. By contrast, the non-paddling transmembrane proteins are sorted out and do not undergo this process of internal recycling through vesicular transport. “This recycling of the cell membrane is studied intensively by the community working on intracellular vesicular traffic, but its role in motility was hardly considered,” Theodoly says. “These functions of protein sorting and trafficking seemed highly sophisticated for swimming. Our investigations, to our own surprise, bridge such distant domains as the physics of microswimmers and the biology of vesicular traffic.” The authors say that molecular paddling could allow immune cells to thoroughly explore all locations in the body as they migrate in liquid-filled niches such as swollen body parts, infected bladders, cerebrospinal fluid, or amniotic fluid. Moving forward, the researchers plan to investigate the functions of molecular paddling in various environments and assess whether other types of cells use this mode of migration. Reference: “Amoeboid Swimming Is Propelled by Molecular Paddling in Lymphocytes” by Laurene Aoun, Alexander Farutin, Nicolas Garcia-Seyda, Paulin Nègre, Mohd Suhail Rizvi, Sham Tlili, Solene Song, Xuan Luo, Martine Biarnes-Pelicot, Rémi Galland, Jean-Baptiste Sibarita, Alphée Michelot, Claire Hivroz, Salima Rafai, Marie-Pierre Valignat, Chaouqi Misbah and Olivier Theodoly, 11 August 2020, Biophysical Journal. DOI: 10.1016/j.bpj.2020.07.033 The work was supported by the French Agence Nationale de la Recherche, the LABEX INFORM, the Région Sud, the Turing Centre for Living systems, the Excellence Initiative of Aix-Marseille University-A*MIDEX, a French ”Investissements d’Avenir” program, and the company Alveole. Senescent cells, or “zombie cells,” are unique in that they ultimately cease multiplying but do not die off as expected. Researchers have found a new pathway for the buildup of “zombie cells,” which promote aging. Senescent cells, or cells that have lost their ability to divide, increase with age and are major contributors to age-related illnesses such as cancer, dementia, and cardiovascular disease. In a new study, a team led by the University of Pittsburgh and UPMC Hillman Cancer Center researchers discovered a method through which senescent, or “zombie,” cells develop. Patricia Opresko, Ph.D., professor of environmental and occupational health and of pharmacology and chemical biology at the University of Pittsburgh and co-leader of the Genome Stability Program at UPMC Hillman Cancer Center. Credit: Patricia Opresko The study, which was recently published in the journal Nature Structural & Molecular Biology, demonstrates for the first time that oxidative damage to telomeres — the protecting tips of chromosomes that behave like plastic caps at the end of a shoelace — can cause cellular senescence. These discoveries might ultimately result in new treatments that promote healthy aging or fight cancer. “Zombie cells are still alive, but they can’t divide, so they don’t help replenish tissues,” said senior author Patricia Opresko, Ph.D., professor of environmental and occupational health and of pharmacology and chemical biology at Pitt. “Although zombie cells don’t function properly, they’re not couch potatoes — they actively secrete chemicals that promote inflammation and damage neighboring cells. Our study helps answer two big questions: How do senescent cells accumulate with age, and how do telomeres contribute to that?” When a healthy human cell divides to create two identical cells, a little bit of DNA is shaved off the tip of each chromosome, causing telomeres to get shorter with each division. However, it is unknown if a cell may divide so often in a person’s lifetime that its telomeres fully degrade, resulting in a zombie-like condition. For decades, scientists have known that telomere shortening causes senescence in lab-grown cells, but they could only assume that DNA damage at telomeres could convert cells into zombies. This hypothesis could not previously be tested since the techniques used to damage DNA were non-specific, creating lesions across the entire chromosome. “Our new tool is like a molecular sniper,” explained first author Ryan Barnes, Ph.D., a postdoctoral fellow in Opresko’s lab. “It creates oxidative damage exclusively at the telomeres.” X-shaped chromosomes are stained purple, and telomeres appear as green spots at chromosome tips. When researchers used a novel tool to induce oxidative damage specifically at telomeres, they can become fragile (green arrows), sending cells into senescence. The inset shows an enlarged chromosome with fragile telomeres, indicated by multiple green spots at chromosome tips. Credit: Barnes et al., Nature Structural & Molecular Biology, (2022) To develop such marksman-like precision, the team used a special protein that binds exclusively to telomeres. This protein acts like a catcher’s mitt, grabbing hold of light-sensitive dye “baseballs” that the researchers tossed into the cell. When activated with light, the dye produces DNA-damaging reactive oxygen molecules. Because the dye-catching protein binds only to telomeres, the tool creates DNA lesions specifically at chromosome tips. Accelerated Senescence Due to Telomere Damage Ryan Barnes, Ph.D., a postdoctoral fellow at the University of Pittsburgh. Credit: Ryan Barnes Using human cells grown in a dish, the researchers found that damage at telomeres sent the cells into a zombie state after just four days — much faster than the weeks or months of repeated cell divisions that it takes to induce senescence by telomere shortening in the lab. “We found a new mechanism for inducing senescent cells that is completely dependent on telomeres,” explained Opresko, who also co-leads the Genome Stability Program at UPMC Hillman. “These findings also solve the puzzle of why dysfunctional telomeres are not always shorter than functional ones.” Sunlight, alcohol, smoking, poor diet, and other factors generate reactive oxygen molecules that damage DNA. Cells have repair pathways to patch up DNA lesions, but, according to Opresko, telomeres are “exquisitely sensitive” to oxidative damage. The researchers found that damage at telomeres disrupted DNA replication and induced stress signaling pathways that led to senescence. Potential for New Interventions and Senolytic Drugs “Now that we understand this mechanism, we can start to test interventions to prevent senescence,” said Barnes. “For example, maybe there are ways to target antioxidants to the telomeres to protect them from oxidative damage.” The findings could also inform the development of new drugs called senolytics that home in on zombie cells and kill them. “By reducing the accumulation of zombie cells, which contribute to degenerative diseases, we might be able to promote ‘healthspan’ — the length of time that a person is healthy,” he added. Reference: “Telomeric 8-oxo-guanine drives rapid premature senescence in the absence of telomere shortening” by Ryan P. Barnes, Mariarosaria de Rosa, Sanjana A. Thosar, Ariana C. Detwiler, Vera Roginskaya, Bennett Van Houten, Marcel P. Bruchez, Jacob Stewart-Ornstein and Patricia L. Opresko, 30 June 2022, Nature Structural & Molecular Biology. DOI: 10.1038/s41594-022-00790-y New images of the SIRT6 sirtuin enzyme—which regulates aging and other metabolic processes—help explain how it is able to access genetic material within the cell. This cryo-electron microscopy map shows the enzyme in complex with the nucleosome, a tightly packed complex of DNA and proteins called histones. Credit: Song Tan Lab, Penn State Penn State researchers have revealed how sirtuin enzymes interact with nucleosomes to regulate aging and metabolic processes. Their findings, using cryo-electron microscopy, may inform drug discovery efforts targeting sirtuins for biomedical applications. New scientific research provides insight into how an enzyme that helps regulate aging and other metabolic processes accesses our genetic material to modulate gene expression within the cell. A team led by Penn State researchers has produced images of a sirtuin enzyme bound to a nucleosome—a tightly packed complex of DNA and proteins called histones—showing how the enzyme navigates the nucleosome complex to access both DNA and histone proteins and clarifying how it functions in humans and other animals. A paper describing the results was published on April 14 in the journal Science Advances. Sirtuins are a type of enzyme found in organisms ranging from bacteria to humans that play important roles in aging, sensing DNA damage, and suppressing tumors in various cancers. Because of these varied roles, pharmaceutical companies are exploring their potential for biomedical applications. Much effort has focused on the ability of some sirtuins to decrease gene expression by removing a chemical flag from histone proteins. Nucleosomes in Gene Expression “In our cells, DNA is not naked like we see it in textbooks; it is spooled around proteins called histones within a large complex called the nucleosome,” said Song Tan, Verne M. Willaman Professor of Molecular Biology at Penn State and an author of the paper. “This packaging can also contribute signals for turning on or turning off genes: Adding an ‘acetyl’ chemical flag to the histone packaging material turns on a gene, while removing the acetyl flag turns the gene off. Sirtuins can silence gene activity by removing the acetyl flag from histones packaged into nucleosomes. Understanding how sirtuins interact with the nucleosome to remove this flag could inform future drug discovery efforts.” Previous studies have focused on how sirtuins interact with short segments of histones in isolation, in part because such histone “tail” peptides are much easier to work with in the lab. According to Tan, the nucleosome is a hundred times larger than typical histone peptides used in these studies and are consequently much more complicated to work with. “We have visualized a sirtuin enzyme called SIRT6 on its physiologically relevant substrate—the entire nucleosome,” said Jean-Paul Armache, assistant professor of biochemistry and molecular biology at Penn State and an author of the paper. “And we found that SIRT6 interacts with multiple parts of the nucleosome, not only the histone where the acetyl flag is to be modified.” Using a powerful type of imaging called cryo-electron microscopy with instruments at the Penn State Cryo-Electron Microscopy Facility, the National Cancer Institute, and the Pacific Northwest Cryo-EM Center, the researchers identified how SIRT6 positions itself on the nucleosome in order to remove an acetyl group from the K9 position on the histone called H3. Following up with biochemical experiments—in collaboration with the lab of Craig Peterson at the University of Massachusetts Chan Medical School—helped confirm their results. Arginine Anchor The researchers found that SIRT6 binds to the nucleosome using a type of connection called an “arginine anchor.” This type of binding—described by Tan’s lab in 2014—is used by a variety of proteins that target a particularly acidic patch on the nucleosome’s surface. In this case, a structural feature of SIRT6 called an extended loop nestles into a divot in the acidic patch, somewhat like a pipe sitting in a ditch. “The arginine anchor is a common paradigm for how many chromatin proteins interact with the nucleosome,” said Tan. “When we mutated the SIRT6 arginine anchor, the activity at the K9 position was severely affected, supporting a critical role for the SIRT6’s arginine anchor. Surprisingly, this mutation also impacted SIRT6’s enzymatic activity at a different position, K56, located much further away.” Instead of SIRT6 binding to the nucleosome in two different ways to access the two different histone positions, it is possible that SIRT6 binds to access K9 in a way that might also provide access to K56. “SIRT6 binds to a partially unwrapped nucleosome, with DNA displaced from the end of the nucleosome,” said Armache. “This exposes the K56 position, and it is possible that SIRT6 could essentially lean down to reach that position. We would like to validate this hypothesis in the future. We also hope to explore how SIRT6 works alongside other enzymes and to better understand its role in the response to DNA damage.” Reference: “Cryo-EM structure of the human Sirtuin 6–nucleosome complex” by Un Seng Chio, Othman Rechiche, Alysia R. Bryll, Jiang Zhu, Erik M. Leith, Jessica L. Feldman, Craig L. Peterson, Song Tan and Jean-Paul Armache, 14 April 2023, Science Advances. DOI: 10.1126/sciadv.adf7586 In addition to Tan, Armache, and Peterson, the research team at Penn State includes postdoctoral scholars Un Seng Chio, Othman Rechiche, and Jiang Zhu and graduate student Erik Leith. The research team at the UMass Chan Medical School also includes Alysia Bryll and Jessica Feldman. This research was supported by the U.S. National Institutes of Health and the Pennsylvania Department of Health using Tobacco CURE funds. RRG455KLJIEVEWWF |
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