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Nucleic Acids Research, 1986, Vol. 14, No. 14 5827-5841
© 1986

Articles

Secondary structure model for mouse ßMaj globin mRNA derived from enzymatic digestion data, comparative sequence and computer analysis

Raymond E. Lockard, Kathleen Currey1, Michelle Browner2, Charles Lawrence2 and Jacob Maizel3

Department of Biochemistry, Cornell University Medical College 1300 York Avenue, New York, NY 10021 1Department of Neurology, University of Utah Salt Lake City, UT 84132 2Department of Cell Biology, Baylor College of Medicine One Baylor Plaza, Houston, TX 77030 3Laboratory of Mathematical Biology, National Cancer Institute-FCRF Frederick, MD 21701, USA

Received February 27, 1986. Revised May 21, 1986. Accepted May 21, 1986.

A model for the secondary structure of mouse ßMaj globin messenger RNA is presented based on enzymatic digestion data, comparative sequence and computer analysis. Using 5'-32P-end-labeled ß globin mRNA as a substrate, single-stranded regions were determined with S1 and T1 nucleases and double-stranded regions with V1 ribonuclease from cobra venom. The structure data obtained for ca. 75% of the molecule was introduced into a computer algorithm which predicts secondary structures of minimum free energy consistent with the enzymatic data. Two prominent base paired regions independently derived by phylogenetic analysis were also present in the computer generated structure lending support for the model. An interesting feature of the model is the presence of long-range base pairing interactions which permit the ß globin mRNA to fold back on itself, thereby bringing the 5'- and 3'-noncoding regions within close proximity. This feature is consistent with data from other laboratories suggesting an interaction of the 5'- and 3'-domains in the mammalian globin mRNAs.


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