EXPRESSION & FUNCTION OF ORGANELLE HEAT SHOCK PROTEINS

表达

• 批准号: 3301613
• 负责人: Elizabeth Vierling
• 金额: $ 15.05万
• 依托单位: UNIVERSITY OF ARIZONA
• 依托单位国家: 美国
• 财政年份: 1989
• 资助国家: 美国
• 起止时间: 1989-07-01 至 1994-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3301613
• 关键词: Arabidopsis; Leguminoseae; cell growth regulation; chloroplasts; developmental genetics; eukaryote; gene expression; genes; immunocytochemistry; messenger RNA; mitochondria; molecular cloning; organelles; plant genetics; plant growth /development; protein sequence; protein structure function; stress; stress proteins

Most eukaryotic and prokaryotic cells respond to high temperature and certain other stresses with the production of heat shock proteins (HSPs). The HSPs are evolutionarily conserved proteins hypothesized to be essential for survival during stress, or recovery from stress. HSP functions are also known to participate in normal cell growth and development. Very recently, it has been found that specific HSPs are localized to semiautonomous eukaryotic organelles, the mitochondria and chloroplasts. These organelle HSPs are homologous to previously characterized HSPs found in the cytoplasm or nucleus. I have cloned and sequenced the gene for a major, 21 kDa nuclear-encoded chloroplast HSP which is homologous to eukaryotic cytoplasmic low molecular weight HSPs. I have also identified two high molecular weight (63 and 100 kDa) chloroplast HSPs. The proposed research will examine the expression and function of the 21 kDa chloroplast HSP, and further characterize the 63 and 100 kDa chloroplast HSPs. Our long term goals are to determine the function of organelle HSPs at the molecular level, and to better understand their role in the cellular physiology of eukaryotic responses to the environment. Complementary molecular, biochemical and genetic approaches will be used to investigate the role of organelle HSPs. The biochemical properties of HSP21, its interaction with other proteins and intra- organelle distribution will be examined. The expression of HSP21 mRNA and protein will be studied under a range of physiological stress conditions and during normal development. As an additional approach to determining organelle HSP function, mutagenized population of Arabidopsis plants will be screened to identify HSP21 deficient mutants. The phenotype of these mutants will be examined during both normal growth and high temperature stress. Studies of the 63 and 100 kDa HSPs will be initiated, including cloning and sequencing of corresponding cDNAs. In summary, the production of organelle-localized HSPs is a newly discovered component of the stress response and normal developmental program of eukaryotic cells. The proposed studies with further our knowledge of this fundamental aspect of cellular biochemistry.

大多数真核和原核细胞对高温有反应 以及某些其他应力， 蛋白质（HSPs）。 热休克蛋白是进化上保守的蛋白质 假设是在压力下生存所必需的，或 从压力中恢复过来。 已知HSP功能也参与 正常细胞生长和发育。 最近， 发现特异性热休克蛋白定位于半自主真核生物 线粒体和叶绿体。 这些细胞器 热休克蛋白与先前在大肠杆菌中发现的特征性热休克蛋白同源。 细胞质或细胞核。 我克隆并测序了 主要的，21 kDa的核编码的叶绿体HSP，其是同源的 真核细胞质低分子量热休克蛋白。 我也 鉴定了两个高分子量（63和100 kDa）叶绿体 HSP。 拟议的研究将检查表达和 21 kDa叶绿体HSP的功能，并进一步表征 63和100 kDa叶绿体HSPs。 我们的长期目标是 在分子水平上确定细胞器热休克蛋白的功能， 为了更好地了解它们在细胞生理学中的作用， 真核生物对环境的反应 互补的分子、生物化学和遗传学方法将 用于研究细胞器热休克蛋白的作用。 生化 热休克蛋白21的性质，它与其他蛋白质的相互作用， 将检查细胞器分布。 HSP21的表达 mRNA和蛋白质将在一系列生理条件下进行研究。 在正常的发展过程中，在正常的发展过程中。 作为附加 确定细胞器HSP功能的方法，诱变的 将筛选拟南芥植物群体以鉴定HSP 21 缺陷突变体 将检查这些突变体的表型 在正常生长和高温胁迫下。 研究 将启动63和100 kDa HSP，包括克隆和 相应cDNA的测序。 总之，细胞器定位的热休克蛋白的产生是一个新的 发现的压力反应和正常的组成部分 真核细胞的发育程序。 拟议的研究 随着我们对细胞的基本方面的进一步了解， 生物化学