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秀丽隐杆线虫中组织蛋白酶D推定结构基因的鉴定。

Identification of a putative structural gene for cathepsin D in Caenorhabditis elegans.

作者信息

Jacobson L A, Jen-Jacobson L, Hawdon J M, Owens G P, Bolanowski M A, Emmons S W, Shah M V, Pollock R A, Conklin D S

机构信息

Department of Biological Sciences, University of Pittsburgh, Pennsylvania 15260.

出版信息

Genetics. 1988 Jun;119(2):355-63. doi: 10.1093/genetics/119.2.355.

Abstract

Mutants of Caenorhabditis elegans having about 10% of wild-type activity of the aspartyl protease cathepsin D have been isolated by screening. Mutant homozygotes have normal growth rates and no obvious morphological or developmental abnormalities. The mutant gene (cad-1) has been mapped to the right extremity of linkage group II. Heterozygous animals (cad-1/+) show intermediate enzyme levels and animals heterozygous for chromosomal deficiencies of the right extremity of linkage group II have 50% of wild-type activity. Cathepsin D purified from a mutant strain has a lower activity per unit mass of pure enzyme. These data suggest that cad-1 is a structural gene for cathepsin D.

摘要

通过筛选,已分离出具有约10%野生型天冬氨酸蛋白酶组织蛋白酶D活性的秀丽隐杆线虫突变体。突变纯合子具有正常的生长速率,且无明显的形态或发育异常。突变基因(cad-1)已被定位到连锁群II的右端。杂合动物(cad-1/+)显示出中等酶水平,而连锁群II右端染色体缺失的杂合动物具有50%的野生型活性。从突变菌株中纯化的组织蛋白酶D每单位质量纯酶的活性较低。这些数据表明cad-1是组织蛋白酶D的一个结构基因。

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本文引用的文献

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Ultra-rapid fluorescent labelling of proteins.蛋白质的超快速荧光标记
Nature. 1962 Jan 13;193:167-8. doi: 10.1038/193167b0.
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Annu Rev Biochem. 1980;49:63-91. doi: 10.1146/annurev.bi.49.070180.000431.
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Analysis of proteinase A function in yeast.酵母中蛋白酶A功能的分析。
Eur J Biochem. 1981 Dec;121(1):47-52. doi: 10.1111/j.1432-1033.1981.tb06427.x.
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Annu Rev Biochem. 1982;51:335-64. doi: 10.1146/annurev.bi.51.070182.002003.

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