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TitleStructures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 116, Issue 49, Page 24507-24516, Year 2019
Publish dateDec 3, 2019
AuthorsNing Jia / Mihaela C Unciuleac / Chaoyou Xue / Eric C Greene / Dinshaw J Patel / Stewart Shuman /
PubMed AbstractMycobacterial AdnAB is a heterodimeric helicase-nuclease that initiates homologous recombination by resecting DNA double-strand breaks (DSBs). The AdnA and AdnB subunits are each composed of an N- ...Mycobacterial AdnAB is a heterodimeric helicase-nuclease that initiates homologous recombination by resecting DNA double-strand breaks (DSBs). The AdnA and AdnB subunits are each composed of an N-terminal motor domain and a C-terminal nuclease domain. Here we report cryoelectron microscopy (cryo-EM) structures of AdnAB in three functional states: in the absence of DNA and in complex with forked duplex DNAs before and after cleavage of the 5' single-strand DNA (ssDNA) tail by the AdnA nuclease. The structures reveal the path of the 5' ssDNA through the AdnA nuclease domain and the mechanism of 5' strand cleavage; the path of the 3' tracking strand through the AdnB motor and the DNA contacts that couple ATP hydrolysis to mechanical work; the position of the AdnA iron-sulfur cluster subdomain at the Y junction and its likely role in maintaining the split trajectories of the unwound 5' and 3' strands. Single-molecule DNA curtain analysis of DSB resection reveals that AdnAB is highly processive but prone to spontaneous pausing at random sites on duplex DNA. A striking property of AdnAB is that the velocity of DSB resection slows after the enzyme experiences a spontaneous pause. Our results highlight shared as well as distinctive properties of AdnAB vis-à-vis the RecBCD and AddAB clades of bacterial DSB-resecting motor nucleases.
External linksProc Natl Acad Sci U S A / PubMed:31740608 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

20440

6ppj

EMDB-20440, PDB-6ppj:
Cryo-EM structure of AdnA(D934A)-AdnB(D1014A) in complex with AMPPNP
Method: EM (single particle) / Resolution: 3.5 Å

20446

6ppr

EMDB-20446, PDB-6ppr:
Cryo-EM structure of AdnA(D934A)-AdnB(D1014A) in complex with AMPPNP and DNA
Method: EM (single particle) / Resolution: 3.5 Å

20447

6ppu

EMDB-20447, PDB-6ppu:
Cryo-EM structure of AdnAB-AMPPNP-DNA complex
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • mycolicibacterium smegmatis (bacteria)
  • mycobacterium smegmatis (bacteria)
  • bacillus subtilis subsp. subtilis str. 168 (bacteria)
  • mycobacterium smegmatis (strain atcc 700084 / mc(2)155) (bacteria)
KeywordsDNA BINDING PROTEIN / DNA BINDING PROTEIN/DNA / DNA / DNA BINDING PROTEIN-DNA complex

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