AMINO TERMINAL PROCESSING OF YEAST PROTEINS

酵母蛋白的氨基末端加工

• 批准号: 6118496
• 负责人: YIE-HWA CHANG
• 金额: $ 0.11万
• 依托单位: WASHINGTON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-08-01 至 1999-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6118496
• 关键词: biomedical resource; parasitism; proteins; spectrometry

Mutant Glutathione-S-Transferases (GST) were expressed and purified from wild-type yeast, map1 yeast, and map2 yeast. Since methionine aminopeptidases (MetAPs) are involved in N-terminal processing, we predict that GSTs expressed in yeast strains lacking either MetAP1 or MetAP2 should not have their N-terminal methionine completely removed. We hope using mass spectrometry to analyze the extent of met-removal of different GSTs to understand the roles of two distinct MetAPs. We are using a series of mutant glutathionine-S-transferases to evaluate the roles of each methionine aminopeptidases in eukaryotic cells.

表达突变的谷胱甘肽-S-转移酶（GST），并 从野生型酵母，MAP1酵母和MAP2酵母中纯化。 自从 N末端参与蛋氨酸氨基肽酶（Metaps） 处理，我们预测在缺乏酵母菌菌株中表达的GST metap1或metap2不应具有其N末端蛋氨酸 完全删除。 我们希望使用质谱法分析 不同GST的满足范围以了解两个的作用 不同的代码。 我们正在使用一系列突变体 谷胱甘肽-S-转移酶以评估每种蛋氨酸的作用 真核细胞中的氨基肽酶。