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. 1996 Mar 1;24(5):835–842. doi: 10.1093/nar/24.5.835

Cleavage by RNase P of gene N mRNA reduces bacteriophage lambda burst size.

Y Li 1, S Altman 1
PMCID: PMC145720  PMID: 8600449

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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