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Nucleic Acids Research, 1985, Vol. 13, No. 11 4097-4112
© 1985


Articles

Variants within the yeast Ty sequence family encode a class of structurally conserved proteins

Alexandra M. Fulton, Jane Mellor, Melanie J. Dobson, John Chester, John R. Warmington1, Keith J. Indge1, Stephen G. Oliver1, Patricia de la Paz2, Wilma Wilson, Alan J. Kingsman* and Susan M. Kingsman

1Department of Biochemistry and Applied Molecular Biology, UMIST P.O. Box 88, Manchester M60 1QD, UK 2Departments of Molecular Biophysics, University of Oxford South Parks Road, Oxford 0X1 3QU Departments of Biochemistry, University of Oxford South Parks Road, Oxford 0X1 3QU

*To whom correspondence should be addressed

Received April 19, 1985. Revised May 10, 1985. Accepted May 10, 1985.

The Ty transposable elements of Saccharomyces cerevisiae form a heterogeneous family within which two broad structural classes (I and II) exist. The two classes differ by two large substitutions and many restriction sites. We show that, like class I elements a class II element, Tyl-17, also appears to contain at least two major protein coding regions, designated TYA and TYB, and the organisational relationship of these regions has been conserved. The TYA genes of both classes encode proteins, designated pl proteins, with an approximate molecular weight of 5Ø Kd and, despite considerable variation between the TYA regions at the DNA level, the structures of these proteins are remarkably similar. These observations strongly suggest that the pl proteins of Ty elements are functionally significant and that they have been subject to selection


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