Intrinsic sequence specificity of the Cas1 integrase directs new spacer acquisition
Rollie, C; Schneider, S; Brinkmann, AS; et al.Bolt, EL; White, MF
Date: 18 August 2015
Article
Journal
eLife
Publisher
eLife Sciences Publications -
Publisher DOI
Abstract
The adaptive prokaryotic immune system CRISPR-Cas provides RNA-mediated
protection from invading genetic elements. The fundamental basis of the system is the ability to
capture small pieces of foreign DNA for incorporation into the genome at the CRISPR locus,
a process known as Adaptation, which is dependent on the Cas1 and Cas2 ...
The adaptive prokaryotic immune system CRISPR-Cas provides RNA-mediated
protection from invading genetic elements. The fundamental basis of the system is the ability to
capture small pieces of foreign DNA for incorporation into the genome at the CRISPR locus,
a process known as Adaptation, which is dependent on the Cas1 and Cas2 proteins. We demonstrate
that Cas1 catalyses an efficient trans-esterification reaction on branched DNA substrates, which
represents the reverse- or disintegration reaction. Cas1 from both Escherichia coli and Sulfolobus
solfataricus display sequence specific activity, with a clear preference for the nucleotides flanking the
integration site at the leader-repeat 1 boundary of the CRISPR locus. Cas2 is not required for this
activity and does not influence the specificity. This suggests that the inherent sequence specificity of
Cas1 is a major determinant of the adaptation process.
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