Abstract
Limited hydrolysis of gene 32 protein by various proteinases results in the production of three stable cleavage products. Two of these products show an affinity for native T4 DNA cellulose that the uncleaved protein does not exhibit. A model for proteolytic cleavage and for the local unwinding of DNA in advance of the replication fork is discussed in terms of this unusual binding affinity.
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Moise, H., Hosoda, J. T4 gene 32 protein model for control of activity at replication fork. Nature 259, 455–458 (1976). https://doi.org/10.1038/259455a0
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DOI: https://doi.org/10.1038/259455a0
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