Source:http://linkedlifedata.com/resource/pubmed/id/21697083
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
35
|
| pubmed:dateCreated |
2011-8-29
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| pubmed:databankReference | |
| pubmed:abstractText |
Clustered regularly interspaced short palindromic repeats (CRISPR) and their associated protein genes (cas genes) are widespread in bacteria and archaea. They form a line of RNA-based immunity to eradicate invading bacteriophages and malicious plasmids. A key molecular event during this process is the acquisition of new spacers into the CRISPR loci to guide the selective degradation of the matching foreign genetic elements. Csn2 is a Nmeni subtype-specific cas gene required for new spacer acquisition. Here we characterize the Enterococcus faecalis Csn2 protein as a double-stranded (ds-) DNA-binding protein and report its 2.7 ? tetrameric ring structure. The inner circle of the Csn2 tetrameric ring is ?26 ? wide and populated with conserved lysine residues poised for nonspecific interactions with ds-DNA. Each Csn2 protomer contains an ?/? domain and an ?-helical domain; significant hinge motion was observed between these two domains. Ca(2+) was located at strategic positions in the oligomerization interface. We further showed that removal of Ca(2+) ions altered the oligomerization state of Csn2, which in turn severely decreased its affinity for ds-DNA. In summary, our results provided the first insight into the function of the Csn2 protein in CRISPR adaptation by revealing that it is a ds-DNA-binding protein functioning at the quaternary structure level and regulated by Ca(2+) ions.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
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| pubmed:issn |
1083-351X
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:day |
2
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| pubmed:volume |
286
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
30759-68
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| pubmed:meshHeading |
pubmed-meshheading:21697083-Amino Acid Sequence,
pubmed-meshheading:21697083-Bacterial Proteins,
pubmed-meshheading:21697083-Cloning, Molecular,
pubmed-meshheading:21697083-Crystallography, X-Ray,
pubmed-meshheading:21697083-DNA,
pubmed-meshheading:21697083-DNA-Binding Proteins,
pubmed-meshheading:21697083-Enterococcus faecalis,
pubmed-meshheading:21697083-Models, Genetic,
pubmed-meshheading:21697083-Models, Molecular,
pubmed-meshheading:21697083-Molecular Conformation,
pubmed-meshheading:21697083-Molecular Sequence Data,
pubmed-meshheading:21697083-Multigene Family,
pubmed-meshheading:21697083-Protein Binding,
pubmed-meshheading:21697083-Protein Structure, Quaternary,
pubmed-meshheading:21697083-Protein Structure, Tertiary,
pubmed-meshheading:21697083-RNA Interference,
pubmed-meshheading:21697083-Sequence Homology, Amino Acid
|
| pubmed:year |
2011
|
| pubmed:articleTitle |
Crystal structure of clustered regularly interspaced short palindromic repeats (CRISPR)-associated Csn2 protein revealed Ca2+-dependent double-stranded DNA binding activity.
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| pubmed:affiliation |
Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14850, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|