Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: Discrimination of Qip1 and Rch1 from hSrp1 by their ability to interact with DNA helicase Q1/RecQL

被引：82

作者：

Seki, T

Tada, S

Katada, T

Enomoto, T

机构：

[1] TOHOKU UNIV,FAC PHARMACEUT SCI,DEPT MOL CELL BIOL,AOBA KU,SENDAI,MIYAGI 98077,JAPAN

[2] UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM,BUNKYO KU,TOKYO 113,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1997年 / 234卷 / 01期

关键词：

D O I：

10.1006/bbrc.1997.6535

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We isolated two cDNA clones encoding human proteins which interact with DNA helicase Q1/RecQL, a human homologue of Escherichia coli RecQ protein, by two-hybrid screening, One of these proteins, named Qip1, was a novel protein homologous to the nuclear localization signal (NLS) receptor importin-alpha, and the other was the known protein Rch1, which is also a homologue of importin-alpha. DNA helicase Q1 in human cell lysates was coprecipitated with bacterially expressed Qip1 and Rch1 fused with glutathione-S-transferase with glutathione Sepharose beads, confirming the interaction between these proteins and DNA helicase Q1. Two-hybrid experiments revealed that Qip1 interacted with the NLS of SV40 T antigen similar to Rch1 and hSrp1. In addition, interaction of the putative NLS in DNA helicase Q1 with Qip1 and Rch1 but not with hSrp1 was confirmed by the two-hybrid system. (C) 1997 Academic Press.

引用

页码：48 / 53

页数：6

共 29 条

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