| pubmed-article:12417756 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12417756 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:12417756 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:12417756 | lifeskim:mentions | umls-concept:C0036576 | lld:lifeskim |
| pubmed-article:12417756 | lifeskim:mentions | umls-concept:C0073237 | lld:lifeskim |
| pubmed-article:12417756 | lifeskim:mentions | umls-concept:C1418833 | lld:lifeskim |
| pubmed-article:12417756 | lifeskim:mentions | umls-concept:C0600499 | lld:lifeskim |
| pubmed-article:12417756 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:12417756 | lifeskim:mentions | umls-concept:C1707761 | lld:lifeskim |
| pubmed-article:12417756 | pubmed:dateCreated | 2002-11-13 | lld:pubmed |
| pubmed-article:12417756 | pubmed:abstractText | RNase E, a multifunctional endoribonuclease of Escherichia coli, attacks substrates at highly specific sites. By using synthetic oligoribonucleotides containing repeats of identical target sequences protected from cleavage by 2'-O-methylated nucleotide substitutions at specific positions, we investigated how RNase E identifies its cleavage sites. We found that the RNase E catalytic domain (i.e., N-Rne) binds selectively to 5'-monophosphate RNA termini but has an inherent mode of cleavage in the 3' to 5' direction. Target sequences made uncleavable by the introduction of 2'-O-methyl-modified nucleotides bind to RNase E and impede cleavages at normally susceptible sites located 5' to, but not 3' to, the protected target. Our results indicate that RNase E can identify cleavage sites by a 3' to 5' "scanning" mechanism and imply that anchoring of the enzyme to the 5'-monophosphorylated end of these substrates orients the enzyme for directional cleavages that occur in a processive or quasiprocessive mode. In contrast, we find that RNase G, which has extensive structural homology with and size similarity to N-Rne, and can functionally complement RNase E gene deletions when overexpressed, has a nondirectional and distributive mode of action. | lld:pubmed |
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| pubmed-article:12417756 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12417756 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12417756 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12417756 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12417756 | pubmed:author | pubmed-author:CohenStanley... | lld:pubmed |
| pubmed-article:12417756 | pubmed:author | pubmed-author:FengYananY | lld:pubmed |
| pubmed-article:12417756 | pubmed:author | pubmed-author:VickersTimoth... | lld:pubmed |
| pubmed-article:12417756 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12417756 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12417756 | pubmed:pagination | 14746-51 | lld:pubmed |
| pubmed-article:12417756 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12417756 | pubmed:articleTitle | The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection. | lld:pubmed |
| pubmed-article:12417756 | pubmed:affiliation | Department of Genetics, Stanford University School of Medicine, CA 94305USA-5120, USA. | lld:pubmed |
| entrez-gene:945641 | entrezgene:pubmed | pubmed-article:12417756 | lld:entrezgene |
| entrez-gene:947744 | entrezgene:pubmed | pubmed-article:12417756 | lld:entrezgene |
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