TY - JOUR
T1 - A myosin-like dimerization helix and an extra-large homeodomain are essential elements of the tripartite DNA binding structure of LFB1
AU - Nicosia, Alfredo
AU - Monaci, Paolo
AU - Tomei, Licia
AU - De Francesco, Raffaele
AU - Nuzzo, Maurizio
AU - Stunnenberg, Hendrik
AU - Cortese, Riccardo
N1 - Funding Information:
We wish to thank lain Mattaj, Angus Lamond, Roberto Di Lauro, Helen Francis Lang, Valeria Poli, and Huw Parry for critical reading of the manuscript. We are grateful to Dr. P Vecchio of the Dipartimento Chi-mica degli Ormoni (CNR), Milano, for the use of the spectropolarimeter. G. Paolella helped us in the preparation of Figure 9. We also thank P Neuner and S. Weston for oligonucleotide synthesis, P Riedinger for figure preparation, and H. Seifert for typing the manuscript. Synthetic peptides were kindly provided by H. Gausepohl. L. T. is a recipient of a European Economic Community fellowship and R. D. F. of a long-term EMBO fellowship. This work was supported in part by a grant from the EEC (BAP-0115-D).
PY - 1990/6/29
Y1 - 1990/6/29
N2 - The transcription activator LFB1 is a major determinant of hepatocyte-specific expression of many genes. To study the mechanisms underlying LFB1 transcriptional selectivity, we have initiated its biochemical characterization. By in vitro complementation assays we have defined two distinct regions required for high levels of transcription, which resemble previously described activation domains. In contrast, the region of LFB1 necessary for DNA binding displays several novel features. The DNA binding domain is tripartite, including a homeodomain of unusual length (81 amino acids) and an N-terminal helix similar to part of myosin. This helical region mediates dimerization, which is shown to be essential for DNA binding.
AB - The transcription activator LFB1 is a major determinant of hepatocyte-specific expression of many genes. To study the mechanisms underlying LFB1 transcriptional selectivity, we have initiated its biochemical characterization. By in vitro complementation assays we have defined two distinct regions required for high levels of transcription, which resemble previously described activation domains. In contrast, the region of LFB1 necessary for DNA binding displays several novel features. The DNA binding domain is tripartite, including a homeodomain of unusual length (81 amino acids) and an N-terminal helix similar to part of myosin. This helical region mediates dimerization, which is shown to be essential for DNA binding.
UR - http://www.scopus.com/inward/record.url?scp=0025281219&partnerID=8YFLogxK
U2 - 10.1016/0092-8674(90)90687-A
DO - 10.1016/0092-8674(90)90687-A
M3 - Article
C2 - 2364427
AN - SCOPUS:0025281219
SN - 0092-8674
VL - 61
SP - 1225
EP - 1236
JO - Cell
JF - Cell
IS - 7
ER -