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J. Biol. Chem., Vol. 255, Issue 23, 11484-11493, Dec, 1980
RL Burke, BM Alberts and J Hosoda
The proteolytic removal of about 60 amino acids from the COOH terminus of
the bacteriophage T4 helix-destabilizing protein (gene 32 protein) produces
32*I, a 27,000-dalton fragment which still binds tightly and cooperatively
to single-stranded DNA. The substitution of 32*I protein for intact 32
protein in the seven-protein T4 replication complex results in dramatic
changes in some of the reactions catalyzed by this in vitro DNA replication
system, while leaving others largely unperturbed. 1. Like intact 32
protein, the 32*I protein promotes DNA synthesis by the DNA polymerase when
the T4 polymerase accessory proteins (gene 44/62 and 45 proteins) are also
present. The host helix- destabilizing protein (Escherichia coli ssb
protein) cannot replace the 32I protein for this synthesis. 2. Unlike
intact 32 protein, 32*I protein strongly inhibits DNA synthesis catalyzed
by the T4 DNA polymerase alone on a primed single-stranded DNA template. 3.
Unlike intact 32 protein, the 32*I protein strongly inhibits RNA primer
synthesis catalyzed by the T4 gene 41 and 61 proteins and also reduces the
efficiency of RNA primer utilization. As a result, de novo DNA chain starts
are blocked completely in the complete T4 replication system, and no
lagging strand DNA synthesis occurs. 4. The 32*I protein does not bind to
either the T4 DNA polymerase or to the T4 gene 61 protein in the absence of
DNA; these associations (detected with intact 32 protein) would therefore
appear to be essential for the normal control of 32 protein activity, and
to account at least in part for observations 2 and 3, above. We propose
that the COOH-terminal domain of intact 32 protein functions to guide its
interactions with the T4 DNA polymerase and the T4 gene 61 RNA-priming
protein. When this domain is removed, as in 32*I protein, the helix
destabilization induced by the protein is controlled inadequately, so that
polymerizing enzymes tend to be displaced from the growing 3'-OH end of a
polynucleotide chain and are thereby inhibited. Eukaryotic
helix-destabilizing proteins may also have similar functional domains
essential for the control of their activities.
Proteolytic removal of the COOH terminus of the T4 gene 32 helix- destabilizing protein alters the T4 in vitro replication complex
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