Building a replisome from interacting pieces: sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex

Article Abstract:

The sliding clamp of the bacteriophage RB69 is discussed related to its complexation to a peptide from DNA polymerase and a polymerase editing complex. The complex is essential for DNA polymerase interactions. The DNA polymerase is complexed with primer-template DNA. It appears that a replication inhibitor protein acts by competing with eukaryotic polymerases for the same binding pocket on the clamp.

author: Shamoo, Yousif, Steitz, Thomas
DNA, Eukaryotic cells, Cells (Biology), Eukaryotes, Bacteriophages, DNA polymerases

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Single active site catalysis of the successive phosphoryl transfer steps by DNA transposases: insights from phosphorothioate stereoselectivity

Article Abstract:

Insights from phosphorothioate stereoselectivity have helped promote understanding of single active site catalysis of the successive phosphoryl transfer steps by DNA transposases. The phosphorothioate stereoselectivity at the scissile position has been studied for the four reaction steps catalyzed by the Tn10 transposase.

author: Kennedy, A.K., Haniford, D.B., Mizuuchi, K.
Chirality, Binding sites (Biochemistry), Active sites (Biochemistry), Stereochemistry

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p53AIP1, a potential mediator of p53-dependent apoptosis, and its regulation by Ser-46-phosphorylated p53

Article Abstract:

A novel gene designated p53AIP1 (p53-regulated Apoptosis-Inducing Protein 1), localized in mitochondria, has been isolated using direct cloning of p53 binding sequences from human genomic DNA. The gene is a potential mediator of p53-dependent apoptosis. Its regulation by Ser-46-phosphorylated p53 is discussed.

author: Matsuda, K., Oda, K., Arakawa, H., Tanaka, T., Tanikawa, C., Mori, T., Nishimori, H., Tamai, K., Tokino, T., Nakamura. Y., Taya, Y.
Japan, Genetic aspects, Cell death, Genetic regulation, Mitochondria

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subjects list: Statistical Data Included, Research, United States, Physiological aspects, Cytochemistry, Phosphorylation
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