T4 gene 32 protein model for control of activity at replication fork
- 1 February 1976
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 259 (5543), 455-458
- https://doi.org/10.1038/259455a0
Abstract
Limited hydrolysis of gene 32 protein [of bacteriophage T4] by various proteinases results in the production of 3 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.Keywords
This publication has 15 references indexed in Scilit:
- Gene 21 protein-dependent proteolysis in vitro of purified gene 22 product of bacteriophage T4Journal of Molecular Biology, 1975
- Studies of the self-association of bacteriophage T4 gene 32 protein by equilibrium sedimentationJournal of Molecular Biology, 1975
- Denaturation of T4 DNA by an in vitro processed gene 32‐proteinFEBS Letters, 1974
- Regulation of the synthesis of bacteriophage T4 gene 32 proteinJournal of Molecular Biology, 1974
- Analysis of bacteriophage T7 early RNAs and proteins on slab gelsJournal of Molecular Biology, 1973
- Stimulation of T4 bacteriophage DNA polymerase by the protein product of T4 gene 32Journal of Molecular Biology, 1971
- T4 Bacteriophage Gene 32: A Structural Protein in the Replication and Recombination of DNANature, 1970
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Molecular mechanisms of genetic recombination in bacteriophageJournal of Molecular Biology, 1966
- Physiological Studies of Conditional Lethal Mutants of Bacteriophage T4DCold Spring Harbor Symposia on Quantitative Biology, 1963