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Function of the Hydrophobic Transmembrane Portion of Thy‐1 Antigen
Author(s) -
Tate Genshu
Publication year - 1990
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.1990.tb01031.x
Subject(s) - biology , antigen , microbiology and biotechnology , mutagenesis , mutant , amino acid , transmembrane protein , transfection , gene , transmembrane domain , biochemistry , site directed mutagenesis , western blot , genetics , receptor
Thy‐1 antigen is anchored in the cell membrane by glycophosphatidyl inositol linkages instead of hydrophobic protein domains. The hydrophobic portion of Thy‐1 antigen is cleaved by putative “transamidase.” Mutated genes were constructed by using site‐directed mutagenesis. One mutant gene codes Thy‐1 antigen lacking carboxy terminal amino acids from 112 Cys to 143 Leu including cell membrane binding amino acid 112 Cys. The other mutant gene codes Thy‐1 antigen lacking from 124 Trp to 143 Leu that includes leucine core portion. DNA transfection analysis and Northern blot analysis revealed that hydrophobic portion of Thy‐1 antigen is essential to express Thy‐1 molecule onto the cell surface.