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Structural Modeling of the PTF1‐J and PTF1‐L Heterotrimeric Transcription Factor Complexes
Author(s) -
Stein Kelly,
Kohrs Alix,
Schuller Lauren,
Marshall Andrea,
MacDonald Raymond,
Coats Ward
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.lb171
Subject(s) - heterotrimeric g protein , transcription factor , transcription (linguistics) , microbiology and biotechnology , biology , genetics , gene , g protein , signal transduction , linguistics , philosophy
Students in Biomedical Research Studies at Hillcrest High School in Dallas, Texas participate in an ongoing research program at the University of Texas Southwestern Medical Center to study the structure and function of a mammalian transcription factor complex. Ptf1a is a sequence specific DNA‐binding transcription factor that is crucial to the development of the embryonic pancreas. Its functional form is in a trimeric complex composed of a common E‐box binding protein (E12/47, HEB, or TCF12), Ptf1a and either Rbpj or Rbpjl. The Rbpj form of the complex (PTF1‐J) is required for the early stage of pancreatic development. Subsequently, the Rbpjl‐form (PTF1‐L) is required for the formation of mature acinar cells. PTF1‐L is involved in an auto‐regulatory loop for the maintenance of transcription of both Ptf1a and Rbpjl genes. We have generated structure models for the PTF1‐J and PTF1‐L heterotrimeric transcription factor complexes bound to their consensus DNA binding sequence. The models provide the orientation of the Ptf1a/E12 heterodimer relative to the Rbpj and Rbpjl proteins and identify the protein surface areas at the heterotrimeric interface.