z-logo
open-access-imgOpen Access
Isolation and characterization of mouse Thy-1 genomic clones.
Author(s) -
H C Chang,
Tetsunori Seki,
Tetsuya Moriuchi,
Jack Silver
Publication year - 1985
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.82.11.3819
Subject(s) - amino acid , cosmid , biology , microbiology and biotechnology , peptide sequence , nucleic acid sequence , gene , rna , exon , sequence analysis , coding region , protein primary structure , biochemistry
The mouse Thy-1.2 gene was isolated from a C57Bl/6 cosmid library and its nucleotide sequence was determined from an 8-kilobase-long EcoRI fragment. The predicted amino acid sequence indicates that the mouse Thy-1 molecule contains a 19 amino acid leader peptide and the 112 amino acids reported previously from protein sequence analysis, plus 31 extra amino acids at the carboxyl terminus. These 31 amino acids contain a stretch of 20 amino acids, at positions 124-143, which is highly hydrophobic. RNA transfer blot analysis of RNA from mouse tissues indicates that the sequence coding for these 31 amino acids is present on poly(A)-containing RNA of brain and thymus tissues. This hydrophobic segment very likely provides the basis for integration of Thy-1 within the plasma membrane. The entire coding sequence of Thy-1 is distributed among three exons, encoding amino acid residues -19 to 8, -7 to 106, and 107 to 143, respectively. Comparison of the mouse and rat Thy-1 genes shows that both have a similar gene organization and encode a highly conserved transmembrane segment.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom