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人类细胞核核糖核酸酶P的一个亚基具有ATP酶活性。

A subunit of human nuclear RNase P has ATPase activity.

作者信息

Li Y, Altman S

机构信息

Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA.

出版信息

Proc Natl Acad Sci U S A. 2001 Jan 16;98(2):441-4. doi: 10.1073/pnas.98.2.441. Epub 2001 Jan 9.

Abstract

Human nuclear RNase P purified from HeLa cells has ATPase activity. This activity is associated with one of the protein subunits of the enzyme, Rpp20. Thus, human nuclear RNase P, which contains several proteins and one essential RNA, has at least one other enzymatic activity in addition to cleavage of phosphoester bonds in RNA. The amino acid sequence of Rpp20 has a signature motif found in an ATPase-containing subunit of a family of protein complexes (ABC transporters) that mediate a variety of trans-membrane traffic, as well as a segment, DIxxN, that resembles the DEAD box motif of many ATPases: together, these might represent an ATPase signature motif.

摘要

从人宫颈癌细胞(HeLa细胞)中纯化出的人源细胞核核糖核酸酶P具有ATP酶活性。该活性与该酶的一种蛋白质亚基Rpp20相关。因此,人源细胞核核糖核酸酶P含有多种蛋白质和一种必需RNA,除了能切割RNA中的磷酸酯键外,还至少具有一种其他酶活性。Rpp20的氨基酸序列具有一个特征基序,该基序存在于一类介导多种跨膜运输的蛋白质复合物(ABC转运蛋白)的含ATP酶亚基中,还有一段类似于许多ATP酶的DEAD盒基序的序列DIxxN:这些共同组成了一个ATP酶特征基序。

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