The Eukaryotic Replication Complex and Its Affinity Modification Analysis |
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Authors: | Lavrik O. I. Khlimankov D. Yu. Khodyreva S. N. |
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Affiliation: | (1) Novosibirsk Institute of Bioorganic Chemistry, Siberian Division, Russian Academy of Sciences, Novosibirsk, 630090, Russia |
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Abstract: | Replication of eukaryotic DNA is performed by a protein complex in which the central part is played by DNA polymerases. Synthesis with eukaryotic DNA polymerases , , and involves various replication factors, including the replication protein A, replication factor C, proliferating cell nuclear antigen, etc. Replication enzymes and factors also participate in DNA repair, which is interrelated with DNA replication. The function of the entire multicomponent system is regulated by protein–nucleic acid and protein–protein interactions. The eukaryotic replication complex was not isolated as a stable supramolecular structure, suggesting its dynamic organization. Hence X-ray analysis and other instrumental techniques are hardly suitable for studying this system. An alternative approach is affinity modification. Its most promising version involves in situ generation of photoreactive DNA replication intermediates. The review considers the recent progress in photoaffinity modification studies of DNA polymerases, eukaryotic replication factors, and their interactions with DNA replication intermediates. |
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Keywords: | DNA replication and repair protein– nucleic acid interactions photoaffinity modification |
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