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Table 1 Enzymes involved in mRNA degradation and modification during T4 infection.

From: Post-transcriptional control by bacteriophage T4: mRNA decay and inhibition of translation initiation

Enzyme

Origin

Reaction catalyzed. Main properties

Role in T4 development

RNase E

E. coli

Endonuclease. Produces 5'-P termini. Activated by 5'-monophosphorylated RNA. Scaffold of the degradosome

Major role in mRNA degradation throughout the phage developmental cycle.

RNase G

E. coli

Endonuclease. Produces 5'-P termini. Activated by 5'- monophosphorylated RNA.

Cuts in the 5' regions of some early RegB processed transcripts.

RegB

T4

Sequence-specific endonuclease. Produces 5'-OH termini. Requires S1 r-protein as co-factor

Inactivates early transcripts by cleaving in Shine-Dalgarno sequences. Expedites early mRNA degradation.

RNase LS

E. coli

Endonuclease. Its activity depends on rnlA and rnlB loci. Associated in a multiprotein compex.

Cleaves within T4 middle and late transcripts and expedites their degradation.

RNase II

RNase R

Polynucleotide phosphorylase

E. coli

3'-5' exonucleases. PNPase requires 3'-OH termini; the other two are indifferent to the nature of the 3' terminus.

Degrade mRNAs. The relative contribution of each RNase has not been determined.

PrrC

E. coli

tRNAlys anticodon nuclease. Normally silent in E. coli but activated by the T4-encoded Stp polypeptide.

Deleterious to T4 propagation if Pnk or Rli1 enzymes are inactivated.

Polynucleotide kinase (PNK)

T4

Phosphorylation of 5'-OH polynucleotide termini. Hydrolysis of 3'-terminal phosphomonoesters and of 2',3'-cyclic phosphodiesters

Counteracts, together with T4 RNA ligase 1, host tRNA anticodon nuclease PrrC. Makes RegB-processed RNA substrates for RNases E and G.

Dmd

T4

An early product that binds the RnlA protein, a member of RNase LS

Antagonist of RNase LS

Poly(A) polymerase

E. coli

Addition of poly(A) tails to the 3' end of RNAs

Probably inactivated after T4 infection

RNA pyrophospho-hydrolase (RppH)

E. coli

Hydrolysis of a pyrophosphate moiety from the 5'-triphosphorylated primary transcripts.

Not yet investigated