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TitleA structural and dynamic model for the assembly of Replication Protein A on single-stranded DNA.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 5447, Year 2018
Publish dateDec 21, 2018
AuthorsLuke A Yates / Ricardo J Aramayo / Nilisha Pokhrel / Colleen C Caldwell / Joshua A Kaplan / Rajika L Perera / Maria Spies / Edwin Antony / Xiaodong Zhang /
PubMed AbstractReplication 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 ...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.
External linksNat Commun / PubMed:30575763 / PubMed Central
MethodsEM (single particle)
Resolution4.7 Å
Structure data

4410

6i52

EMDB-4410, PDB-6i52:
Yeast RPA bound to ssDNA
Method: EM (single particle) / Resolution: 4.7 Å

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • synthetic construct (others)
KeywordsDNA BINDING PROTEIN / Complex / heterotrimer / DNA binding / OB-fold

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