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Science 8 February 1985:
Vol. 227. no. 4687, pp. 649 - 651
DOI: 10.1126/science.2857501
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Articles

Science, Vol 227, Issue 4687, 649-651
Copyright © 1985 by American Association for the Advancement of Science

articles

A hydrophobic transmembrane segment at the carboxyl terminus of thy-1

T Seki, HC Chang, T Moriuchi, R Denome, H Ploegh, and J Silver

The mode of integration of the glycoprotein thy-1 within the cell membrane has been controversial due to an apparent lack of a transmembrane hydrophobic segment. Rat and mouse complementary DNA and genomic clones encoding the thy-1 molecule have been isolated and sequenced. These studies have enabled us to determine the intron-exon organization of the thy-1 gene. Furthermore, they have revealed the existence of a sequence which would encode an extra segment (31 amino acids) at the carboxyl terminus of the thy-1 molecule. These extra amino acids include a 20-amino acid hydrophobic segment which may be responsible for integration of thy-1 within the plasma membrane.


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