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Nucleic Acids Research, 1992, Vol. 20, No. 6 1355-1361
© 1992

MOLECULAR BIOLOGY

An alternatively spliced Pit-1 isoform altered in its ability to trans-activate

Arvia E. Morris, Brian Kloss1, Ruth E. McChesney1, Carter Bancroft1 and Lawrence A. Chasin

Department of Biological Sciences, Columbia University New York, NY 10027, USA 1Department of Physiology and Biophysics, Mount Sinai School of Medicine New York , NY 10029, USA

Although alternative splicing has been shown to give rise to isoforms of a number of transcription factors, such isoforms have not previously been detected for the POU homeodomain protein Pit-1. Screening of a rat pituitary GH3 cell cDNA expression library yielded a clone, termed pCMVPIMa, encoding a 35.8 kO protein (Pit-1 a) containing a 26 amino acid insert in the Pit-1 trans-activation domain. The position of the insert, plus Southern blot analysis, implied that Pit-1 a mRNA arises by alternative splicing of the Pit-1 gene transcript. Pit-1 a mRNA was detected in GH3 rat pituitary tumor cells at levels about 1/7 that of Pit-1 mRNA. Pit-1 a mRNA-specific sequences were also detected In rat and mouse pituitary, and in mouse thyrotropic tumor TtT cells. DNA mobility shift assays showed that Pit-1 a binds specifically to Pit-1 binding sites in the proximal prolactin promoter, but produces DNA-protein complexes of markedly different mobilities than Pit-1. In stably transfected CHO cells which accumulated approximately equal levels of either of the two proteins, Pit-1 trans-activated a prolactin promoter-driven CAT construct, while Pit-1 a yielded no detectable trans-activation, implying a trans-activation ratio for Pit-1 a/Pit-1 of <0.05. Thus, the insertion of 26 amino acids of similar composition into the activation domain of Pit-1 has at once affected both the mode of binding of this protein and its ability to function as a trans-activator.


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