TY - JOUR
T1 - Cleavage by RNase P of gene N mRNA reduces bacteriophage λ burst size
AU - Li, Ying
AU - Altman, Sidney
N1 - Funding Information:
We thank our colleagues, especially Dr C. Guerrier-Takada, for advice, encouragement and exchange of data. This research was supported by grant GM19422 from the National Institutes of Health of the USA.
PY - 1996
Y1 - 1996
N2 - 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.
AB - 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.
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U2 - 10.1093/nar/24.5.835
DO - 10.1093/nar/24.5.835
M3 - Article
C2 - 8600449
AN - SCOPUS:0029984297
SN - 0305-1048
VL - 24
SP - 835
EP - 842
JO - Nucleic acids research
JF - Nucleic acids research
IS - 5
ER -