对脊椎动物 G 蛋白偶联受体融合体进行的硅学分析表明,无论融合体是否具有额外的跨膜序列,都可将其分为三类连接体

IF 1.9 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY The Protein Journal Pub Date : 2024-04-14 DOI:10.1007/s10930-024-10184-2
Toshio Kamiya, Takashi Masuko, Dasiel Oscar Borroto-Escuela, Haruo Okado, Hiroyasu Nakata
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引用次数: 0

摘要

天然的 G 蛋白偶联受体(GPCR)很少有额外的跨膜(TM)螺旋,如人工 TM 连接体,它可以将两个 A 类 GPCR 串联成一条单多肽链(sc)。在这里,我们报告了脊椎动物天然 GPCR 融合体的中间区域存在三组 TM 连接体:(1) 原始共识(即共识 1)和共识 2~4(与 GPCR 本身或其受体相互作用蛋白相关);(2) 共识但与 GPCR 无关的 1~7;(3) 无法应用的 1/2,与任何其他蛋白都没有相似性。硅学分析表明,两栖类的所有天然 GPCR 融合蛋白都缺乏 TM 连接子,爬行动物没有 GPCR 融合蛋白;此外,在脊椎动物(不包括四足动物,即所谓的鱼类)的 GPCR-GPCR 融合蛋白或融合蛋白(GPCR 单体)和非 GPCR 蛋白中,TM 连接子与之前报道的哺乳动物和鸟类序列不同,被归为第 2 组和第 3 组。因此,对之前报道的 TM 链接子进行了排列:共识 1 是[T(I/A/P)(A/S)-(L/N)(I/W/L)(I/A/V)GL(L/G)(A/T)(S/L/G)(I/L)],首次在无脊椎动物海葵 Exaiptasia diaphana 中发现(LOC110241027),在热带鸟类 Opisthocomus hoazin 蛋白质 LOC104327099 中发现(330-SPSFLCI-L-SLL-340)(XP_009930279.1);与 GPCR 相关的共识 2~4 分别是沙漠木鼠 Neotoma lepida A6R68_19462 中的(371-prlilyavfc fgtatg-386)(OBS78147.1)中的(363-lsipfcll yiaallgnfi llfvi-385)、Gavia stellate(红喉鹭)LOC104264164(XP_009819412.1)中的(479-ti vvvymivcvi glvgnflvmy viir-504)和蜗牛鱼 GPCR(TNN80062.在哺乳动物 Neotoma lepida、鸟类 Erythrura gouldiae 和鱼类蛋白质(分别为 OBS83645.1、RLW13346.1 和 KPP79779.1)中,TM 链接子属于第 2 组。 在此,我们首次将天然 TM 链接子归类为所有脊椎动物中的罕见进化事件。
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In Silico Analyses of Vertebrate G-Protein-Coupled Receptor Fusions United With or Without an Additional Transmembrane Sequence Indicate Classification into Three Groups of Linkers

Natural G-protein-coupled receptors (GPCRs) rarely have an additional transmembrane (TM) helix, such as an artificial TM-linker that can unite two class A GPCRs in tandem as a single-polypeptide chain (sc). Here, we report that three groups of TM-linkers exist in the intervening regions of natural GPCR fusions from vertebrates: (1) the original consensus (i.e., consensus 1) and consensus 2~4 (related to GPCR itself or its receptor-interacting proteins); (2) the consensus but GPCR-unrelated ones, 1~7; and (3) the inability to apply 1/2 that show no similarity to any other proteins. In silico analyses indicated that all natural GPCR fusions from Amphibia lack a TM-linker, and reptiles have no GPCR fusions; moreover, in either the GPCR-GPCR fusion or fusion protein of (GPCR monomer) and non-GPCR proteins from vertebrates, excluding tetrapods, i.e., so-called fishes, TM-linkers differ from previously reported mammalian and are avian sequences and are classified as Groups 2 and 3. Thus, previously reported TM-linkers were arranged: Consensus 1 is [T(I/A/P)(A/S)–(L/N)(I/W/L)(I/A/V)GL(L/G)(A/T)(S/L/G)(I/L)] first identified in invertebrate sea anemone Exaiptasia diaphana (LOC110241027) and (330-SPSFLCI–L–SLL-340) identified in a tropical bird Opisthocomus hoazin protein LOC104327099 (XP_009930279.1); GPCR-related consensus 2~4 are, respectively, (371-prlilyavfc fgtatg-386) in the desert woodrat Neotoma lepida A6R68_19462 (OBS78147.1), (363-lsipfcll yiaallgnfi llfvi-385) in Gavia stellate (red-throated loon) LOC104264164 (XP_009819412.1), and (479-ti vvvymivcvi glvgnflvmy viir-504) in a snailfish GPCR (TNN80062.1); In Mammals Neotoma lepida, Aves Erythrura gouldiae, and fishes protein (respectively, OBS83645.1, RLW13346.1 and KPP79779.1), the TM-linkers are Group 2. Here, we categorized, for the first time, natural TM-linkers as rare evolutionary events among all vertebrates.

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来源期刊
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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