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J. Biol. Chem., Vol. 265, Issue 17, 9934-9942, Jun, 1990
G Karsenty and B de Crombrugghe
Type I collagen, a heterotrimeric protein composed of two alpha 1 chains
and one alpha 2 chain, is a major specialized biosynthetic product of
fibroblastic cells. We performed a functional dissection of a mouse alpha 1
(I) collagen promoter segment (between -222 and -80) that displays strong
activity in vitro and in DNA transfection experiments. Four binding sites
for factors present in nuclear extracts of NIH-3T3 fibroblasts were
identified in this promoter segment. One factor, which has the same binding
characteristics as CBF, a heterodimeric CCAAT binding factor that also
binds and activates the coordinately expressed alpha 2(I) collagen
promoter, interacts with the proximal of two CCAAT motifs. A second factor,
designated IF1, binds to two more upstream, adjacent sites (-190 to -170
and -160 to -130). A third factor, designated IF2, makes contact with
several G residues in the distal unit of a 12-base pair exact G-rich repeat
that brackets the proximal CCAAT motif. Binding studies with mutant
oligonucleotides and experiments with purified CBF indicate that the
binding of IF2 is inhibited by CBF. IF2 is a metalloprotein that requires
zinc cations for efficient binding to its recognition site. DNA
transfection experiments using point mutations or small substitution
mutations that abolish binding of the transacting factors to their cognate
elements were performed. A mutation in the proximal IF1 binding site
increases promoter activity 4-fold, a mutation in the IF2 binding site
increases this activity 10-fold and a mutation in the CBF binding site
decreases this activity 4-5-fold. This suggests that IF1 and IF2 act as
transcriptional inhibitors whereas CBF acts as an activator of the alpha
1(I) collagen promoter. We propose that mutually competitive binding of IF2
and CBF could play a role in the control of the alpha 1(I) collagen
promoter.
Two different negative and one positive regulatory factors interact with a short promoter segment of the alpha 1 (I) collagen gene
Department of Molecular Genetics, University of Texas M.D. Anderson Cancer Center, Houston 77030.
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