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A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA.

ABSTRACT: Replication Protein A (RPA), the major eukaryotic single stranded DNA-binding protein, binds to exposed ssDNA to protect it from nucleases, participates in a myriad of nucleic acid transactions and coordinates the recruitment of other important players. RPA is a heterotrimer and coats long stretches of single-stranded DNA (ssDNA). The precise molecular architecture of the RPA subunits and its DNA binding domains (DBDs) during assembly is poorly understood. Using cryo electron microscopy we obtained a 3D reconstruction of the RPA trimerisation core bound with ssDNA (?55?kDa) at ?4.7?Å resolution and a dimeric RPA assembly on ssDNA. FRET-based solution studies reveal dynamic rearrangements of DBDs during coordinated RPA binding and this activity is regulated by phosphorylation at S178 in RPA70. We present a structural model on how dynamic DBDs promote the cooperative assembly of multiple RPAs on long ssDNA.

SUBMITTER: Yates LA 

PROVIDER: S-EPMC6303327 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature

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A structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA.

Yates Luke A LA   Aramayo Ricardo J RJ   Pokhrel Nilisha N   Caldwell Colleen C CC   Kaplan Joshua A JA   Perera Rajika L RL   Spies Maria M   Antony Edwin E   Zhang Xiaodong X  

Nature communications 20181221 1

Replication Protein A (RPA), the major eukaryotic single stranded DNA-binding protein, binds to exposed ssDNA to protect it from nucleases, participates in a myriad of nucleic acid transactions and coordinates the recruitment of other important players. RPA is a heterotrimer and coats long stretches of single-stranded DNA (ssDNA). The precise molecular architecture of the RPA subunits and its DNA binding domains (DBDs) during assembly is poorly understood. Using cryo electron microscopy we obtai  ...[more]

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