![]() Kim Y, Eom SH, Wang J, Lee DS, Suh SW, Steitz TA (1995) Crystal structure of Thermus aquaticus DNA polymerase. Korolev S, Nayal M, Barnes WM, Di Cera E, Waksman G (1995) Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5- Å resolution: structural basis for thermostability. Ollis DL, Brick P, Hamlin R, Xuong NG, Steitz TA (1985) Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Patel PH, Suzuki M, Adman E, Shinkai A, Loeb LA (2001) Prokaryotic DNA polymerase I: evolution, structure, and “base flipping” mechanism for nucleotide selection. Proc Natl Acad Sci USA 65:168–175īebenek K, Joyce CM, Fitzgerald MP, Kunkel TA (1990) The fidelity of DNA synthesis catalyzed by derivatives of Escherichia coli DNA polymerase I. Klenow H, Henningsen I (1970) Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Joyce CM, Steitz TA (1994) Function and structure relationships in DNA polymerase. Johnson KA (1993) Conformational coupling in DNA polymerase fidelity. Freeman, New York, Chapter 12Įchols H, Goodman MF (1991) Fidelity mechanisms in DNA replication. Lodish H, Berk A, Zipursky SL, Matsudaira P, Baltimore D, Darnell J (2000) Molecular cell biology, 4th edn. These results can be tested easily by future experiments and are aid our understanding of the chemomechanical coupling mechanism and polymerization dynamics of high-fidelity DNAP. A small backward force can increase the replication velocity and an optimal backward force exists at which the replication velocity has maximum value with any further increase in the backward force the velocity decreases rapidly. By contrast, the backward force has a large effect on the replication velocity, especially at high dNTP concentration. The replication velocity is nearly independent of the forward force, even at very low dNTP concentration. Replication velocity as a function of the template tension with only one adjustable parameter is in good agreement with the available experimental data. Here, based on our proposed model, we take Klenow fragment as an example to study theoretically the dynamics of high-fidelity DNAPs such as the replication velocity versus different types of external force, i.e., a stretching force on the template, a backward force on the enzyme and a forward force on the enzyme. ![]() ![]() Thus, understanding the chemomechanical coupling mechanism and the effect of external mechanical force on replication velocity are the most fundamental issues for high-fidelity DNAP. During DNA synthesis, high-fidelity DNA polymerase (DNAP) translocates processively along the template by utilizing the chemical energy from nucleotide incorporation. ![]()
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