线粒体前鸟氨酸氨甲酰基转移酶加工所必需但导入非必需的信号序列结构域。
A signal sequence domain essential for processing, but not import, of mitochondrial pre-ornithine carbamyl transferase.
作者信息
Nguyen M, Argan C, Sheffield W P, Bell A W, Shields D, Shore G C
出版信息
J Cell Biol. 1987 May;104(5):1193-8. doi: 10.1083/jcb.104.5.1193.
Abstract
Studies using deletion mutagenesis indicate that a processing recognition site lies proximal to the normal cleavage position between gln32 and ser33 of pre-ornithine carbamyl transferase (pOCT). pOCT cDNA was manipulated to delete codons specifying amino acids 22-30 of the signal sequence. The mutant precursor, designated pOCT delta 22-30, was imported to the matrix compartment by purified mitochondria, but remained largely unprocessed; the low level of processing that was observed did not involve the normal cleavage site. Several manipulations performed downstream of the normal pOCT processing site (deletion, substitution, and hybrid protein constructions) affected neither import nor correct processing. Our data suggest that domains specifying import and processing site recognition may be functionally segregated within the signal peptide; that processing is not requisite for import of pOCT; and that a proximal region, not involving the normal signal peptide cleavage site, is required for processing site recognition.
摘要
利用缺失诱变技术进行的研究表明，在鸟氨酸氨甲酰基转移酶前体（pOCT）的谷氨酰胺32和丝氨酸33之间的正常切割位置附近存在一个加工识别位点。对pOCT cDNA进行操作，删除指定信号序列第22 - 30位氨基酸的密码子。将这种突变前体命名为pOCT delta 22 - 30，纯化的线粒体可将其导入线粒体基质区室，但大部分仍未被加工；所观察到的低水平加工并不涉及正常的切割位点。在正常pOCT加工位点下游进行的几种操作（缺失、替换和杂交蛋白构建）既不影响导入也不影响正确加工。我们的数据表明，指定导入和加工位点识别的结构域在功能上可能在线粒体信号肽内是分离的；pOCT的导入不需要加工；并且加工位点识别需要一个不涉及正常信号肽切割位点的近端区域。
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本文引用的文献
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Processing of pre-ornithine transcarbamylase requires a zinc-dependent protease localized to the mitochondrial matrix.鸟氨酸转氨甲酰酶前体的加工需要一种定位于线粒体基质的锌依赖性蛋白酶。
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