塑LPAT1是一种完整的内包膜蛋白,其乙转移酶域位于流体中
Chun-Wei Yu1,2, Van C Nguyen3, Niña Alyssa M Barroga3,4
1Institute of Molecular Biology, Academia Sinica, Taipei, 11529, Taiwan.
Plant cell reports
|October 9, 2024
概括
Lysophosphatidic 酸乙转移酶 1 (LPAT1) 对于植物叶绿体中的银河脂质合成至关重要. 这项研究揭示了LPAT1.
科学领域:
- 植物分子生物学 植物分子生物学
- 叶绿体生物学 叶绿体生物学
- 脂质生物合成 脂质生物合成
背景情况:
- 银河脂质对光合作用膜至关重要.
- lysophosphatidic 酸乙转移酶 1 (LPAT1) 参与了它们的合成.
- 在此之前,LPAT1在叶绿体内的精确定位和拓学是未知的.
研究的目的:
- 确定LPAT1.1的亚质局部和膜拓.
- 为了阐明成熟LPAT1及其过境的尺寸.
- 了解LPAT1在甘油脂生物合成途径中的作用.
主要方法:
- 使用LPAT1前蛋白进行体外翻译和进口试验.
- 用LPAT1-金星融合蛋白构建和补充一个Arabidopsis lpat1淘汰突变物.
- 在分离的叶绿体上进行蛋白酶处理和性提取.
主要成果:
- LPAT1具有至少85个残留物的过境.
- LPAT1定位在质体内膜的内膜上.
- N终端的跨膜域定LPAT1,N终端位于膜间空间,C终端的催化域位于层体.
结论:
- LPAT1的拓与其细菌同类物质PlsC.不同.
- 这种局部化对于理解甘油脂生物合成和潜在的工程应用至关重要.
- 这些发现提供了对质体内的代谢物流的洞察.
相关概念视频
Protein Transport to the Inner Chloroplast Membrane
2.1K
Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
2.1K
Protein Transport to the Outer Chloroplast Membrane
1.9K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
1.9K
Protein Transport to the Stroma
1.8K
Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
1.8K
Protein Transport to the Thylakoids
2.2K
Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
2.2K
Phosphoinositides and PIPs
8.5K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
8.5K
The Inner Mitochondrial Membrane
3.3K
The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria. In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
3.3K


