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FOR THE RECORD

A reinterpretation of the dimerization interface of the N-terminal Domains of STATs

¹ Department of Biochemistry and Molecular Biology, The University of Texas, M.D. Anderson Cancer Center, Houston, Texas 77030, USA
² Howard Hughes Medical Institute, Departments of Molecular and Cell Biology and of Chemistry, University of California, Berkeley, Berkeley, California 94720, USA
³ Forschungsinstitut für Molekulare Pharmacologie, 13125 Berlin, Germany
⁴ Department of Molecular Biology, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA
⁵ The Rockefeller University, New York, New York 10021, USA
⁶ Physical Bioscience Division, Lawrence Berkeley National Lab, Berkeley, California 94720, USA

Reprint requests to: John Kuriyan, 401 Barker Hall MC 3202, Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA; e-mail: kuriyan{at}uclink.berkeley.edu; fax: (510) 643-2352.

The crystal structures of the N-terminal domain (N-domain) and the core region of the STAT family of transcription factors have been determined previously. STATs can form cooperative higher order structures (tetramers or higher oligomers) while bound to DNA. The crystal packing in the STAT4 N-domain crystal structure, determined at 1.5 Å resolution, suggests two alternate organizations of the N-domain dimer. We now present the results of site directed mutagenesis of residues predicted to be involved at each dimer interface. Our results indicate that the dimer interface suggested earlier as being physiologically relevant is, in fact, unlikely to be so. Given the alternative model for the N-domain dimer, the ability of the N-domain to mediate interactions of two STAT dimers on DNA remains unchanged.

Keywords: STAT; dimerization; cooperative DNA binding

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