| pubmed-article:8600449 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8600449 | lifeskim:mentions | umls-concept:C0031298 | lld:lifeskim |
| pubmed-article:8600449 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:8600449 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:8600449 | lifeskim:mentions | umls-concept:C0035696 | lld:lifeskim |
| pubmed-article:8600449 | lifeskim:mentions | umls-concept:C0073243 | lld:lifeskim |
| pubmed-article:8600449 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
| pubmed-article:8600449 | lifeskim:mentions | umls-concept:C0456389 | lld:lifeskim |
| pubmed-article:8600449 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:8600449 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8600449 | pubmed:dateCreated | 1996-5-1 | lld:pubmed |
| pubmed-article:8600449 | pubmed:abstractText | RNase P, an enzyme essential for tRNA biosynthesis, can be directed to cleave any RNA when the target RNA is in a complex with a short, complementary oligonucleotide called an external guide sequence (EGS). RNase P from Escherichia coli can cleave phage lambda N mRNA in vitro or in vivo when the mRNA is in a complex with an EGS. The EGS can either be separate from or covalently linked to M1 RNA, the catalytic RNA subunit of RNase P. The requirement for Mg2+ in the reaction in vitro is lower when the EGS is covalently linked to M1 RNA. Substrates made of DNA can also be cleaved by RNase P in vitro in complexes with RNA EGSs. When either kind of EGS construct is used in vivo, burst size of phage lambda is reduced by > or = 40%. Reduction in burst size depends on efficient expression of the EGS constructs. The product of phage lambda gene N appears to function in a stoichiometric fashion. | lld:pubmed |
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| pubmed-article:8600449 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8600449 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8600449 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8600449 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8600449 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:8600449 | pubmed:author | pubmed-author:AltmanSS | lld:pubmed |
| pubmed-article:8600449 | pubmed:author | pubmed-author:LUMM | lld:pubmed |
| pubmed-article:8600449 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8600449 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8600449 | pubmed:volume | 24 | lld:pubmed |
| pubmed-article:8600449 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8600449 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8600449 | pubmed:pagination | 835-42 | lld:pubmed |
| pubmed-article:8600449 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8600449 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8600449 | pubmed:articleTitle | Cleavage by RNase P of gene N mRNA reduces bacteriophage lambda burst size. | lld:pubmed |
| pubmed-article:8600449 | pubmed:affiliation | Department of Biology, Yale University, New Haven, CT 06520, USA. | lld:pubmed |
| pubmed-article:8600449 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8600449 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:947634 | entrezgene:pubmed | pubmed-article:8600449 | lld:entrezgene |
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