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(Received for publication, September 27, 1994; and in revised form, December 21, 1994) We previously reported the purification and characterization of
the polyhedrin promoter-binding protein (PPBP), an unusual DNA-binding
protein that interacts with transcriptionally important motifs of the
baculovirus polyhedrin gene promoter (S. Burma, B. Mukherjee, A. Jain,
S. Habib, and S.E. Hasnain, J. Biol. Chem.(1994) 269,
2750-2757. PPBP also exhibits a sequence-specific single-stranded
DNA-binding activity. Gel retardations and competition analyses with
double- and single-stranded oligonucleotides indicated that PPBP binds
the coding strand and not the noncoding strand of the promoter. This
was further confirmed by UV cross-linking and Southwestern blotting
experiments. Gel retardations with mutated oligonucleotides indicated
that both dsDNA and ssDNA binding involve common AATAAATAAGTATT motifs.
However, ssDNA binding is dependent upon ionic interactions unlike
dsDNA binding, which is mainly through nonionic interactions. The
affinity of PPBP for the coding strand appears to be higher than that
for duplex promoter DNA. Interestingly, the PPBP-coding strand complex
has a longer half-life (
Volume 270,
Number 9,
Issue of March 3, 1995 pp. 4405-4411
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Initiator
of the
Baculovirus Polyhedrin Promoter Also Binds Specifically to the Coding
Strand
60 min) than the PPBP-duplex promoter
complex (15 min). PPBP represents a unique example of an
``initiator'' promoter-binding protein with dual dsDNA and
ssDNA binding activities, and this reconciles very well with the
unusual binding characteristics displayed by it. The formation of the
PPBP-coding strand complex in vivo may be a crucial step for
the exceptionally high and repeated rounds of transcriptional activity
of the baculovirus polyhedrin gene promoter.
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