Document Detail

Mutational analysis of the COOH-terminal hydrophobic domain of bovine liver 5'-nucleotidase as a signal for glycosylphosphatidylinositol (GPI) anchor attachment.
MedLine Citation:
PMID:  8142426     Owner:  NLM     Status:  MEDLINE    
In order to address the minimum domain of the COOH-terminal hydrophobic region responsible for GPI modification of bovine liver 5'-nucleotidase, we constructed a series of the deletion mutants of the COOH-terminus and expressed them in COS cells. Cells transfected by the deletion mutant of 6 amino acids (-IIILYQ) from the hydrophobic domain (-FSLIFLSVLAVIII-LYQ) did not show any elevation of cell surface-associated 5'-nucleotidase activity, whereas the 2 (-YQ) or 4 (-ILYQ) amino acid deletion mutant retained the bovine liver-derived activity on the cell surface as a GPI-anchored protein. Loss of half the hydrophobic domain (6 or 8 amino acids) resulted in accumulation of the activity in the cell. On the other hand, deletion of the whole hydrophobic domain (17 amino acids) or the entire cleaved-off domain (25 amino acids) made the product secreted into the medium. In conclusion, the hydrophobicity of 13 amino acids in length was enough for the GPI modification of the bovine liver 5'-nucleotidase.
Y Furukawa; H Tamura; H Ikezawa
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1190     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1994 Mar 
Date Detail:
Created Date:  1994-04-29     Completed Date:  1994-04-29     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  273-8     Citation Subset:  IM    
Department of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Nagoya City University, Japan.
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MeSH Terms
5'-Nucleotidase / genetics*,  metabolism*
Amino Acid Sequence
Base Sequence
Cell Line
DNA Mutational Analysis
Glycosylphosphatidylinositols / metabolism*
Liver / enzymology*
Molecular Sequence Data
Peptides / genetics*,  metabolism
Reg. No./Substance:
0/Glycosylphosphatidylinositols; 0/Peptides; EC'-Nucleotidase

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