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

Ying Li, Sidney Altman

Research output: Contribution to journalArticlepeer-review

17 Scopus citations


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 coil can cleave phage λ 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 λ is reduced by ≥ 40%. Reduction in burst size depends on efficient expression of the EGS constructs. The product of phage λ gene N appears to function in a stoichiometric fashion.

Original languageEnglish (US)
Pages (from-to)835-842
Number of pages8
JournalNucleic acids research
Issue number5
StatePublished - 1996
Externally publishedYes

ASJC Scopus subject areas

  • Genetics


Dive into the research topics of 'Cleavage by RNase P of gene N mRNA reduces bacteriophage λ burst size'. Together they form a unique fingerprint.

Cite this