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

O. I. Lavrik; D. M. Kolpashchikov; H. P. Nasheuer; K. Weisshart; A. Favre

doi:10.1016/S0014-5793(98)01544-0

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

O. I. Lavrik, D. M. Kolpashchikov, H. P. Nasheuer, K. Weisshart, A. Favre

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

32 Citations (Scopus)

Abstract

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 β 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 stronlgly dependent upon the length of the template extension. Copyright (C) 1998 Federation of European Biochemical Societies.

Original language	English
Pages (from-to)	186-190
Number of pages	5
Journal	FEBS Letters
Volume	441
Issue number	2
DOIs	https://doi.org/10.1016/S0014-5793(98)01544-0
Publication status	Published - 18 Dec 1998
Externally published	Yes

Keywords

Human replication protein A
Photoaffinity labeling
Photoreactive dNTP derivative
Protein-nucleic acid recognition

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10.1016/S0014-5793(98)01544-0

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

abstract = "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 β 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 stronlgly dependent upon the length of the template extension. Copyright (C) 1998 Federation of European Biochemical Societies.",

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doi = "10.1016/S0014-5793(98)01544-0",

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T1 - Alternative conformations of human replication protein A are detected by crosslinks with primers carrying a photoreactive group at the 3'-end

AU - Lavrik, O. I.

AU - Kolpashchikov, D. M.

AU - Nasheuer, H. P.

AU - Weisshart, K.

AU - Favre, A.

PY - 1998/12/18

Y1 - 1998/12/18

N2 - 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 β 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 stronlgly dependent upon the length of the template extension. Copyright (C) 1998 Federation of European Biochemical Societies.

AB - 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 β 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 stronlgly dependent upon the length of the template extension. Copyright (C) 1998 Federation of European Biochemical Societies.

KW - Human replication protein A

KW - Photoaffinity labeling

KW - Photoreactive dNTP derivative

KW - Protein-nucleic acid recognition

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U2 - 10.1016/S0014-5793(98)01544-0

DO - 10.1016/S0014-5793(98)01544-0

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AN - SCOPUS:0032414605

SN - 0014-5793

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JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

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

Abstract

Keywords

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