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Nucleic Acids Research, 1992, Vol. 20, No. 10 2565-2572
© 1992

MOLECULAR BIOLOGY

Bipartite structure of the downstream element of the mouse beta globin (major) poly(A) signal

Jing S. Chen and Jeffrey L. Nordstrom*

Department of Biological Sciences, Fordham University Bronx, NY 10458, USA

* To whom correspondence should be addressed

Received December 12, 1991. Revised April 13, 1992. Accepted April 13, 1992.

The downstream region of the mouse beta (major) globin poly(A) signal was mutated and analyzed for function in transfected COS cells. From analysis of unidirectional BaI31 deletions, the 3' boundary of the downstream element was defined as +22 (22 nucleotides downstream from the cleavage site). Analysis of cluster mutations, in which 5 or 6 adjacent bases were replaced with a random CA-containing sequence in a manner that did not alter spacing, confirmed +22 as the 3' boundary of the downstream element. The analysis also revealed two short UG-rich sequences, located from +5 to +10 and from +17 to +22, as major functional components. In contrast, a more refined series of mutations, in which clusters of 3 bases were replaced, failed to cause loss of function. We conclude that the downstream element of the mouse beta globin poly(A) signal is bipartite in structure, and that portions of its sequence are functionally redundant.


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