PRMT9, A Novel Protein Arginine Methyltransferase

PRMT9，一种新型蛋白质精氨酸甲基转移酶

基本信息

批准号：
7475671
负责人：
Cecilia Zurita
金额：
$ 2.97万
依托单位：
UNIVERSITY OF CALIFORNIA LOS ANGELES
依托单位国家：
美国
项目类别：
财政年份：
2006
资助国家：
美国
起止时间：
2006-09-30 至 2010-09-29
项目状态：
已结题

来源：
https://reporter.nih.gov/project-details/7475671
关键词：
Acids Amino Acid Sequence Amino Acids Arginine Autoradiography Biochemical Biological Biological Assay Brain Cations Cell Line Cell membrane Cell physiology Cells Chimeric Proteins Class Collecting Cell Column Chromatography Cytolysis DNA Repair Enzymes Family Family member Fellowship Fluorescence Microscopy Genes Glutathione S-Transferase Glycine Goals Green Fluorescent Proteins Hela Cells Homocysteine Homocystine Human Human Genome Hydrolase Hydrolysis In Vitro Incubated Individual Label Lead Libraries Link Mass Spectrum Analysis Measurable Membrane Membrane Proteins Methionine Methods Methylation Methyltransferase Modification Modification Type N-terminal Names Nitrogen Northern Blotting Open Reading Frames Pathway interactions Pattern Physiological Post-Translational Protein Processing Process Protein Array Protein-Arginine N-Methyltransferase Proteins Proteome Purpose RNA Processing RNA Splicing Radioactivity Reaction Regulation Role S-Adenosylmethionine Side Signal Transduction Site Specificity Spottings Standards of Weights and Measures Substrate Specificity Sulfur Tissues Transcriptional Regulation Transport Process Tumor Suppressor Proteins arginine methyltransferase density expectation fibrillarin human tissue in vivo inhibitor/antagonist member methyl group novel periodate-oxidized adenosine polyvinylidene fluoride protein expression repaired research study

项目摘要

DESCRIPTION (provided by applicant): Each of the nine current members of the protein arginine methyltransferase (PRMT) family has substrates whose differential methylations can lead to distinct physiological changes in the cell. However, although many in vivo substrates have been identified, many others have not. For example, the substrates of PRMT2 have not been characterized due to lack of measurable activity. Cellular roles that have been established in arginine methylation include the involvement of RNA splicing, processing and transport, transcriptional controls, DNA repair, and intracellular signaling. This proposal will set forth specific aims to characterize the newest member of the methyltransferase family, PRMT9. The first step would be to determine enzyme specificity of methylable substrates. Once the substrates are identified, and PRMT9 is characterized by its type of methyltransferase activity, I will determine its localization and its tissue expression pattern. These results will contribute to our understanding of the overall significance of methyltransferases in cellular processes.

描述（由申请人提供）：蛋白质精氨酸甲基转移酶（PRMT）家族的九个当前成员中的每一个都具有底物，其差异甲基化可以导致细胞中不同的生理变化。然而，尽管许多体内底物已被鉴定，但许多其他底物尚未鉴定。例如，由于缺乏可测量的活性，PRMT2 的底物尚未被表征。精氨酸甲基化已确定的细胞作用包括 RNA 剪接、加工和运输、转录控制、DNA 修复和细胞内信号传导。该提案将提出具体目标来描述甲基转移酶家族最新成员 PRMT9 的特征。第一步是确定可甲基化底物的酶特异性。一旦确定了底物，并且 PRMT9 通过其甲基转移酶活性类型进行表征，我将确定其定位及其组织表达模式。这些结果将有助于我们理解甲基转移酶在细胞过程中的整体重要性。