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Literature summary for 4.6.1.25 extracted from

  • Juskauskas, A.; Zajanckauskaite, A.; Meskys, R.; Ger, M.; Kaupinis, A.; Valius, M.; Truncaite, L.
    Interaction between phage T4 protein RIII and host ribosomal protein S1 inhibits endoribonuclease RegB activation (2022), Int. J. Mol. Sci., 23, 9483.
    View publication on PubMed
Search for more literature for 4.6.1.25

Activating Compound

Activating Compound Comment Organism Structure
Escherichia coli host ribosomal protein S1 S1 acts as a cofactor of the T4 phage RegB endoribonuclease. S1 binds RNA substrates and promotes cleavage by RegB. Direct interaction between phage T4 protein RIII and Escherichia coli host ribosomal protein S1 inhibits endoribonuclease RegB activation. The 70 kDa RIII protein mainly targets the 5th domain of S1. RIII interacts with S1 at a molar ratio of 1:1 Tequatrovirus T4

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type an dmutant enzymes in Escherichia coli strain BL21 (DE3), subcloning in Escherichia coli strain DH10B Tequatrovirus T4

Protein Variants

Protein Variants Comment Organism
additional information construction of a T4 DELTAregB single mutant and a T4 DELTArIIIDELTAregB double mutant Tequatrovirus T4

Inhibitors

Inhibitors Comment Organism Structure
phage T4 protein RIII direct interaction between phage T4 protein RIII and Escherichia coli host ribosomal protein S1 inhibits endoribonuclease RegB activation. The 70 kDa RIII protein mainly targets the 5th domain of S1. RIII interacts with S1 at a molar ratio of 1:1 Tequatrovirus T4

Organism

Organism UniProt Comment Textmining
Tequatrovirus T4 P13312
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Synonyms

Synonyms Comment Organism
endoribonuclease RegB
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 Tequatrovirus T4
RegB
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 Tequatrovirus T4
RegB endoribonuclease
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 Tequatrovirus T4

Cofactor

Cofactor Comment Organism Structure
additional information during T4 phage infection, S1 host protein acts as a cofactor of the T4 phage RegB endoribonuclease. S1 binds RNA substrates and promotes cleavage by RegB of the partially structured AG-rich RNAs and unstructured RNA having an 11-nucleotide-conserved sequence. The minimal domain combination required for stimulation of RegB nuclease is D4-D5, whereas the peptide containing all C-terminal domains (D3-D4-D5-D6) stimulates RegB to the same extent as the full-length protein Tequatrovirus T4

General Information

General Information Comment Organism
additional information the recombinant protein RIII of T4 copurifies with the host ribosomal protein S1 in stoichiometric amounts Tequatrovirus T4
physiological function protein RIII is known as a cytoplasmic antiholin, which plays a role in the lysis inhibition function of T4. Protein RIII also acts as a viral effector protein mainly targeting Escherichia coli host S1 RNA-binding domains that are central for all the activities of this multifunctional protein. ribosomal protein S1 is the largest (61 kDa) flexible protein of the ribosome complex. The S1-RIII interaction prevents the S1-dependent activation of endoribonuclease RegB. During T4 phage infection, S1 acts as a cofactor of the T4 phage RegB endoribonuclease. S1 binds RNA substrates and promotes cleavage by RegB of the partially structured AG-rich RNAs and unstructured RNA having an 11-nucleotide-conserved sequence. The minimal domain combination required for stimulation of RegB nuclease is D4-D5, whereas the peptide containing all C-terminal domains (D3-D4-D5-D6) stimulates RegB to the same extent as the full-length protein. The activity of RNase RegB is limited to the early period of T4 infection, it is deactivated by protein RIII Tequatrovirus T4