在酵母中的CYSTM (CYSPD) 蛋白的棕化
María Luz Giolito1, Gonzalo Bigliani1, Rocío Meinero1
1Centro de Investigaciones en Química Biológica de Córdoba (CIQUIBIC), CONICET, Universidad Nacional de Córdoba, Córdoba, Argentina; Departamento de Química Biológica Ranwel Caputto, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Córdoba, Argentina.
The Journal of biological chemistry
|December 30, 2023
概括
半氨酸跨膜蛋白是棕化,而不是跨膜,并局部化到血膜. 棕化对它们的膜结合和稳定性至关重要,影响它们的降解途径.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 细胞生物学 细胞生物学
背景情况:
- 半氨酸跨膜蛋白在真核生物中保存,在病原体耐药性和金属解毒方面具有已知的作用.
- 酵母成员 (YBR016W,YDL012C,YDR034W-B,YDR210W) 在分子层面上以前没有表征.
- 假定C端的氨酸丰富的基因是一个跨膜域.
研究的目的:
- 在分子水平上对酵母氨酸转膜蛋白质进行表征.
- 为了研究C端的氨酸丰富基因的作用.
- 阐明这些蛋白质的翻译后修饰和局部化.
主要方法:
- 蛋白质的表征和后翻译性修饰的识别 (棕细胞化).
- 使用显微镜进行亚细胞局部化研究.
- 在缺乏特定棕甲基转移酶 (Erf2,Akr1) 和E3结合酶 (Rsp5) 的酵母突变体中分析蛋白质降解途径.
主要成果:
- Ybr016w,Ydr034w-b和Ydr210w是棕化蛋白质,现在分别被称为Cpp1,CPP3和CPP2.
- 这些蛋白质定位到等离子体膜,其极性取决于内细胞分裂和循环.
- 棕化,而不是C端基基因,调解了膜结合,这表明重新命名为富含氨酸的棕化域.
- Erf2的损失导致Cpp1的部分降解,而Akr1的损失导致完全降解.
- 蛋白酶依赖和Rsp5依赖途径中的Cpp1降解不仅仅是由于缺乏棕化.
结论:
- 富含氨酸的C端子域是一个棕细胞化域,而不是一个跨膜域.
- 棕化对于这些蛋白质的膜结合和稳定性至关重要.
- 独特的棕甲基转移酶和降解途径调节这些蛋白质的细胞水平.
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