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FEBS Lett. 1998 Dec 18;441(2):186-90.

Alternative conformations of human replication protein A are detected by crosslinks with primers carrying a photoreactive group at the 3'-end.

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Novosibirsk Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences.


To analyze the influence of single-stranded template extension of DNA duplex on the conformation of human replication protein A (RPA) bound to DNA we have designed two template-primer systems differing by the size of the single-stranded template tail (9 and 19 nucleotides (nt)). Base-substituted photoreactive dUTP analogs were used as substrates for elongation of radiolabeled template-primer by DNA polymerase beta in the absence or in the presence of RPA. Following UV-crosslinking it was demonstrated that the pattern of RPA subunit labeling and consequently RPA arrangement near the 3'-end of the primer is strongly dependent upon the length of the template extension.

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