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.
We isolated two cDNA clones encoding human proteins which interact with DNA helicase Q1/RecQL, a human homologue of Eschelichia 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.
Mesh Terms:
Adenosine Triphosphatases, Amino Acid Sequence, Blotting, Western, Carrier Proteins, Cloning, Molecular, DNA Helicases, Escherichia coli, Gene Expression, Glutathione, Humans, Karyopherins, Molecular Sequence Data, Nuclear Localization Signals, Nuclear Proteins, Protein Binding, RecQ Helicases, Saccharomyces cerevisiae, Sepharose, Sequence Alignment, Sequence Analysis, alpha Karyopherins
Adenosine Triphosphatases, Amino Acid Sequence, Blotting, Western, Carrier Proteins, Cloning, Molecular, DNA Helicases, Escherichia coli, Gene Expression, Glutathione, Humans, Karyopherins, Molecular Sequence Data, Nuclear Localization Signals, Nuclear Proteins, Protein Binding, RecQ Helicases, Saccharomyces cerevisiae, Sepharose, Sequence Alignment, Sequence Analysis, alpha Karyopherins
Biochem. Biophys. Res. Commun.
Date: May. 08, 1997
PubMed ID: 9168958
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