Molecular genetics of Intracellular Protein Transport
细胞内蛋白质运输的分子遗传学
基本信息
- 批准号:7342117
- 负责人:
- 金额:$ 33.12万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:1992
- 资助国家:美国
- 起止时间:1992-02-01 至 2009-08-31
- 项目状态:已结题
- 来源:
- 关键词:AddressBindingBiochemicalBiochemical GeneticsBiochemistryBiological AssayBiological ProcessCaenorhabditis elegansCell physiologyCellsChemistryClassConditionCoupledCysteineDiagnosisDisulfidesEndoplasmic ReticulumEnzymesEukaryotaEukaryotic CellExtracellular ProteinExtracellular SpaceGene ProteinsGene SilencingGenerationsGeneticGenetic ScreeningGenomicsGiardiaGiardia lambliaGlutathioneIsoenzymesLaboratoriesLifeLinkMammalian CellMembraneMethodsMolecular GeneticsObject AttachmentOrganismOrthologous GeneOxidantsOxidasesOxidation-ReductionPathway interactionsPeptidesProcessProtein Complex SubunitProtein Disulfide IsomeraseProtein FamilyProteinsResearchRoentgen RaysSaccharomyces cerevisiaeSourceSpecificitySulfhydryl CompoundsThinkingWorkYeastscDNA Librarycrosslinkdesigndisulfide bondglutathione transporterin vitro Assayinsightinterestintracellular protein transportoxidationparallel processingparalogous genepolypeptideprotein foldingprotein structureresearch studysecretory protein
项目摘要
DESCRIPTION (provided by applicant): The endoplasmic reticulum (ER) is the compartment where membrane and secretory proteins are modified, folded, and assembled. Part of the folding process for most extracellular proteins includes formation of disulfide bonds which can add stability to folded polypeptides and can link subunits of protein complexes. The formation of disulfide bonds requires both enzymes for the generation of disulfide bonds in the lumen of the ER as well as a pathway for the transfer of these bonds to substrate proteins. Dr. Kaiser's research group proposes a combination of biochemical, structural, and genetic experiments in the yeast S. cerevisiae to give fundamental insight into the mechanisms of disulfide bond formation in living cells. Previous work in Dr. Kaiser's laboratory has delineated the core pathway in the ER for protein disulfide bond formation in which a luminal oxidase Ero1p (or Erv2p) transfers a disulfide bond to protein disulfide isomerase (PDI) which in turn transfers its disulfide bond to a substrate protein. Structural studies of Ero1p and Erv2p reveal that although these proteins are not similar in sequence, they nevertheless share key structural features giving insight into the mechanisms by which disulfide bonds are generated and transferred from one protein to another. In this application, Dr. Kaiser proposes to determine how disulfide bonds are selectively transferred from Ero1p to PDI. Additional experiments are designed to understand how the functions of ER oxidases are integrated into the redox biochemistry of the cell. Studies of disulfide bond formation in yeast will be extended to understand interesting disulfide bond forming processes in other organisms including G. lamblia and C. elegans.
In S. cerevisiae it will be possible to apply the full power of a well developed genetic organism to uncover the genes and proteins responsible protein folding in the ER. A detailed understanding of these pathways in S. cerevisiae will make it possible to understand parallel processes in mammalian cells, opening the way to diagnose dysfunctional folding in the ER of mammalian cells and providing new opportunities to control the assembly and secret on of extracellular proteins.
描述(由申请人提供):内质网(ER)是膜和分泌蛋白修饰、折叠和组装的隔室。大多数细胞外蛋白的折叠过程的一部分包括二硫键的形成,二硫键可以增加折叠多肽的稳定性,并可以连接蛋白质复合物的亚基。二硫键的形成需要在ER腔中产生二硫键的酶以及将这些键转移到底物蛋白的途径。凯泽博士的研究小组提出了一个结合生物化学,结构和遗传实验的酵母S。酿酒酵母,使基本的洞察机制的二硫键形成活细胞。Kaiser博士实验室以前的工作已经描绘了ER中蛋白质二硫键形成的核心途径,其中管腔氧化酶Ero1p(或Erv2p)将二硫键转移到蛋白质二硫键异构酶(PDI),后者又将其二硫键转移到底物蛋白质。Ero1p和Erv2p的结构研究表明,尽管这些蛋白质在序列上不相似,但它们具有关键的结构特征,从而可以深入了解二硫键的产生和从一种蛋白质转移到另一种蛋白质的机制。在本申请中,Kaiser博士建议确定二硫键如何选择性地从Ero1p转移到PDI。额外的实验旨在了解ER氧化酶的功能如何整合到细胞的氧化还原生物化学中。酵母中二硫键形成的研究将扩展到了解其他生物体中有趣的二硫键形成过程,包括G。lamblia和C.优雅的
In S.通过研究酿酒酵母,将有可能应用发育良好的遗传生物的全部力量来揭示ER中负责蛋白质折叠的基因和蛋白质。对S.酿酒酵母将使了解哺乳动物细胞中的平行过程成为可能,开辟诊断哺乳动物细胞ER功能失调折叠的途径,并提供控制细胞外蛋白组装和分泌的新机会。
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Chris Alan Kaiser其他文献
Chris Alan Kaiser的其他文献
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{{ truncateString('Chris Alan Kaiser', 18)}}的其他基金
REGULATED PROTEIN DELIVERY TO THE PLASMA MEMBRANE
调节蛋白质向质膜的输送
- 批准号:
2872751 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
Molecular Genetics of Regulated Protein Delivery of the Plasma Membrane
质膜调控蛋白质传递的分子遗传学
- 批准号:
7615535 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
Molecular Genetics of Regulated Protein Delivery of the Plasma Membrane
质膜调控蛋白质传递的分子遗传学
- 批准号:
7260984 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
Molecular Genetics of Regulated Protein Delivery of the Plasma Membrane
质膜调控蛋白质传递的分子遗传学
- 批准号:
7410146 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
REGULATED PROTEIN DELIVERY TO THE PLASMA MEMBRANE
调节蛋白质向质膜的输送
- 批准号:
6351233 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
REGULATED PROTEIN DELIVERY TO THE PLASMA MEMBRANE
调节蛋白质向质膜的输送
- 批准号:
7056735 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
REGULATED PROTEIN DELIVERY TO THE PLASMA MEMBRANE
调节蛋白质向质膜的输送
- 批准号:
2459772 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
Molecular Genetics of Regulated Protein Delivery of the Plasma Membrane
质膜调控蛋白质传递的分子遗传学
- 批准号:
7808814 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
REGULATED PROTEIN DELIVERY TO THE PLASMA MEMBRANE
调节蛋白质向质膜的输送
- 批准号:
6151199 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
REGULATED PROTEIN DELIVERY TO THE PLASMA MEMBRANE
调节蛋白质向质膜的输送
- 批准号:
6743688 - 财政年份:1998
- 资助金额:
$ 33.12万 - 项目类别:
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