研究揭示新生蛋白質組裝機制
作者:
小柯機器人發布時間:2021/1/3 15:56:48
德國海德堡大學(ZMBH)分子生物學中心和DKFZ-ZMBH聯盟德國癌症研究中心(DKFZ)Günter Kramer和Bernd Bukau研究組合作取得最新進展。他們那發現相鄰核糖體翻譯的新生蛋白質之間的相互作用驅動同源異構體裝配。相關論文發表在2021年1月1日出版的《科學》雜誌上。
在這項研究中,他們研究了從附近核糖體中出現的兩種新生蛋白質的直接相互作用(co-co組裝)是否構成寡聚體形成的一般機制。他們使用蛋白質組範圍的篩選來檢測新生鏈連接的核糖體對,並鑑定了在人類細胞中共同組裝的數百個同聚物亞基。相互作用是由五個主要結構域類型介導的,其中最常見的是N末端螺旋形線圈。
他們能夠在大腸桿菌中重組核纖層蛋白的co-co組裝,表明二聚體的形成獨立於專用的組裝機制。Co-co組裝可能因此代表了一種有效的方法,可以限制由擴散驅動的組裝途徑造成的蛋白質聚集風險,並確保同工型特異性同聚物的形成。
據悉,將新合成的蛋白質正確組裝成功能性低聚物對於細胞活性至關重要。
附:英文原文
Title: Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly
Author: Matilde Bertolini, Kai Fenzl, Ilia Kats, Florian Wruck, Frank Tippmann, Jaro Schmitt, Josef Johannes Auburger, Sander Tans, Bernd Bukau, Günter Kramer
Issue&Volume: 2021/01/01
Abstract: Accurate assembly of newly synthesized proteins into functional oligomers is crucial for cell activity. In this study, we investigated whether direct interaction of two nascent proteins, emerging from nearby ribosomes (co-co assembly), constitutes a general mechanism for oligomer formation. We used proteome-wide screening to detect nascent chain–connected ribosome pairs and identified hundreds of homomer subunits that co-co assemble in human cells. Interactions are mediated by five major domain classes, among which N-terminal coiled coils are the most prevalent. We were able to reconstitute co-co assembly of nuclear lamin in Escherichia coli, demonstrating that dimer formation is independent of dedicated assembly machineries. Co-co assembly may thus represent an efficient way to limit protein aggregation risks posed by diffusion-driven assembly routes and ensure isoform-specific homomer formation.
DOI: 10.1126/science.abc7151
Source: https://science.sciencemag.org/content/371/6524/57
Science:《科學》,創刊於1880年。隸屬於美國科學促進會,最新IF:41.037