Document Detail


Molecular cloning and characterization of a novel type of regulatory protein (GDI) for smg p25A, a ras p21-like GTP-binding protein.
MedLine Citation:
PMID:  2115118     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
We recently purified to near homogeneity a novel type of regulatory protein for smg p25A, a ras p21-like GTP-binding protein, from bovine brain cytosol. This regulatory protein, named smg p25A GDP dissociation inhibitor (GDI), regulates the GDP-GTP exchange reaction of smg p25A by inhibiting dissociation of GDP from and subsequent binding of GTP to it. In the present studies, we isolated and sequenced the cDNA of smg p25A GDI from a bovine brain cDNA library by using an oligonucleotide probe designed from the partial amino acid sequence of purified smg p25A GDI. The cDNA has an open reading frame that encodes a protein of 447 amino acids with a calculated Mr of 50,565. This Mr is similar to those of the purified smg p25A GDI estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and sucrose density gradient ultracentrifugation, which are about 54,000 and 65,000, respectively. The isolated cDNA is expressed in Escherichia coli, and the encoded protein exhibits GDI activity. smg p25A GDI is hydrophilic overall, except for one hydrophobic region near the N terminus. smg p25A GDI shares low amino acid sequence homology with the Saccharomyces cerevisiae CDC25-encoded protein, which has been suggested to serve as a factor that regulates the GDP-GTP exchange reaction of the yeast RAS2-encoded protein, but not with the beta gamma subunits of GTP-binding proteins having an alpha beta gamma subunit structure, such as Gs and Gi. The smg p25A GDI mRNA was present in various tissues, including not only tissues in which smg p25A was detectable but also tissues in which it was not detectable. This fact has raised the possibility that smg p25A GDI interacts with another G protein in tissues in which smg p25A is absent.
Authors:
Y Matsui; A Kikuchi; S Araki; Y Hata; J Kondo; Y Teranishi; Y Takai
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  10     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  1990 Aug 
Date Detail:
Created Date:  1990-08-22     Completed Date:  1990-08-22     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4116-22     Citation Subset:  IM    
Affiliation:
Research Center, Mitsubishi Kasei Corporation, Yokohama, Japan.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/D90103
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Brain / metabolism
Cattle
Cloning, Molecular / methods
DNA / genetics
Escherichia coli / genetics
GTP-Binding Proteins / genetics*,  isolation & purification,  metabolism
Gene Library
Molecular Sequence Data
Oligonucleotide Probes / chemical synthesis
Oncogene Protein p21(ras) / genetics*
Peptide Mapping
Recombinant Proteins / isolation & purification,  metabolism
Restriction Mapping
Sequence Homology, Nucleic Acid
rap GTP-Binding Proteins
Chemical
Reg. No./Substance:
0/Oligonucleotide Probes; 0/Recombinant Proteins; 9007-49-2/DNA; EC 3.6.1.-/GTP-Binding Proteins; EC 3.6.5.2/Oncogene Protein p21(ras); EC 3.6.5.2/rap GTP-Binding Proteins
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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