小鼠超氧化物歧化酶铜伴侣蛋白(Ccsd)的克隆、定位和人类同源基因定位。

S D Moore, M M Chen, D W Cox
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引用次数: 9

摘要

铜在细胞内不是以自由状态存在,而是始终与金属蛋白结合。特定的金属伴侣护送铜到细胞内的许多目标,提供保护免受细胞内游离铜的毒性作用。许多金属伴侣蛋白已在酵母、小鼠和人类中被鉴定。为了进一步表征小鼠金属伴侣,我们从一个成年小鼠cDNA脑文库中克隆了小鼠Ccsd,包括编码区和5'和3' utr。我们获得了一个1174 -bp的cDNA和一个825-bp的开放阅读框,翻译了一个274个氨基酸的蛋白质,与人类CCS相同86.9%。利用小鼠-仓鼠辐射杂交面板,我们将Ccsd定位到小鼠19号染色体的近端位置。我们利用人-仓鼠辐射杂交面板,将人类CCS定位到11q13(与小鼠19号染色体同源)。人和小鼠金属伴侣蛋白在人体主要组织中普遍表达,但似乎具有不同的转录产物。
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Cloning and mapping of murine superoxide dismutase copper chaperone (Ccsd) and mapping of the human ortholog.

Copper does not exist in a free state within cells but is found consistently bound to metalloproteins. Specific metallochaperones escort copper to numerous targets within the cell, providing protection from the toxic effects of intracellular free copper. Many metallochaperones have been characterized in yeast, mouse, and human. To further characterize mouse metallochaperones, we cloned murine Ccsd from an adult mouse cDNA brain library, including both the coding region and the 5' and 3' UTRs. We obtained a 1,174-bp cDNA with an 825-bp open reading frame, translating a 274 amino acid protein that is 86.9% identical to human CCS. Using a mouse x hamster radiation hybrid panel, we mapped Ccsd to a proximal position on mouse chromosome 19. We mapped human CCS to 11q13 (homologous with mouse chromosome 19), utilizing a human x hamster radiation hybrid panel. The human and mouse metallochaperones are ubiquitously expressed in the major tissues of the body but seem to have different transcription products.

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