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. 1993 Jan;12(1):9–16. doi: 10.1002/j.1460-2075.1993.tb05626.x

The inactive form of recA protein: the 'compact' structure.

R W Ruigrok 1, B Bohrmann 1, E Hewat 1, A Engel 1, E Kellenberger 1, E DiCapua 1
PMCID: PMC413170  PMID: 8428597

Abstract

When recA protein is enzymatically inactive in vitro, it adopts a more compact helical polymer form than that of the active protein polymerized onto DNA in the presence of ATP. Here we describe some aspects of this structure. By cryo-electron microscopy, a pitch of 76 A is found for both the self-polymer and the inactive complex with ssDNA. A smaller pitch of 64 A is observed in conventional electron micrographs. The contour length of complexes with ssDNA was used to estimate the binding stoichiometry in the compact complex, 6 +/- 1 nt/recA. In addition, the compact structure was observed in vivo in Escherichia coli: inclusion bodies produced upon induction of recA expression in an overproducing strain have a fibrous morphology with the structural parameters of the compact polymer.

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Selected References

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