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  The host-encoded RNase E endonuclease as the crRNA maturation enzyme in a CRISPR-Cas subtype III-Bv system.

Behler, J., Sharma, K., Reimann, V., Wilde, A., Urlaub, H., & Hess, W. R. (2018). The host-encoded RNase E endonuclease as the crRNA maturation enzyme in a CRISPR-Cas subtype III-Bv system. Nature Microbiology, 3(3), 367-377. doi:10.1038/s41564-017-0103-5.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-7032-9 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-31B2-C
Genre: Journal Article

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 Creators:
Behler, J., Author
Sharma, K.1, Author              
Reimann, V., Author
Wilde, A., Author
Urlaub, H.1, Author              
Hess, W. R., Author
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1Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              

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Free keywords: Bacterial genetics; RNA
 Abstract: Specialized RNA endonucleases for the maturation of clustered regularly interspaced short palindromic repeat (CRISPR)-derived RNAs (crRNAs) are critical in CRISPR-CRISPR-associated protein (Cas) defence mechanisms. The Cas6 and Cas5d enzymes are the RNA endonucleases in many class 1 CRISPR-Cas systems. In some class 2 systems, maturation and effector functions are combined within a single enzyme or maturation proceeds through the combined actions of RNase III and trans-activating CRISPR RNAs (tracrRNAs). Three separate CRISPR-Cas systems exist in the cyanobacterium Synechocystis sp. PCC 6803. Whereas Cas6-type enzymes act in two of these systems, the third, which is classified as subtype III-B variant (III-Bv), lacks cas6 homologues. Instead, the maturation of crRNAs proceeds through the activity of endoribonuclease E, leaving unusual 13- and 14-nucleotide-long 5'-handles. Overexpression of RNase E leads to overaccumulation and knock-down to the reduced accumulation of crRNAs in vivo, suggesting that RNase E is the limiting factor for CRISPR complex formation. Recognition by RNase E depends on a stem-loop in the CRISPR repeat, whereas base substitutions at the cleavage site trigger the appearance of secondary products, consistent with a two-step recognition and cleavage mechanism. These results suggest the adaptation of an otherwise very conserved housekeeping enzyme to accommodate new substrates and illuminate the impressive plasticity of CRISPR-Cas systems that enables them to function in particular genomic environments.

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Language(s): eng - English
 Dates: 2018-02-052018-03
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41564-017-0103-5
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Title: Nature Microbiology
Source Genre: Journal
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Pages: - Volume / Issue: 3 (3) Sequence Number: - Start / End Page: 367 - 377 Identifier: -