The bacteriophage T4 regB ribonuclease. Stimulation of the purified enzyme by ribosomal protein S1.

Ruckman, Judy; Ringquist, Steven; Brody, Edward N.; Gold, Larry

doi:10.1016/s0021-9258(18)47069-x

Cited by 46 publications

(13 citation statements)

References 42 publications

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“…SI may recognize specific sequences within these RNAs and through protein-protein contacts link them to the translational machinery. Moreover, Ruckman et al (1994) showed that the sequence-specific RNA endonuclease from bacteriophage T4, the product of the regB gene, requires SI for efficient cleavage at GGAG sequences. Sequencespecific binding of RNA by SI protein may provide a general mechanism to regulate gene expression.…”

Section: Ugaafaauuaaacaugmentioning

confidence: 99%

High-Affinity RNA Ligands to Escherichia coli Ribosomes and Ribosomal Protein S1: Comparison of Natural and Unnatural Binding Sites

Ringquist¹,

Jones²,

Snyder³

et al. 1995

Biochemistry

116

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High-affinity RNA ligands were generated against intact 30S ribosomes, S1-depleted 30S ribosomes, and purified ribosomal protein S1. Sequence analysis indicated two classes of ligand: unstructured RNAs containing a Shine-Dalgarno sequence and structured RNAs containing a pseudoknot. The Shine-Dalgarno-containing ligands were generated against S1-depleted 30S ribosomes but, surprisingly, not against intact 30S ribosomes or ribosomal protein S1. In contrast, pseudoknot-containing ligands were generated against intact ribosomes as well as purified S1 protein. The two classes of ligand exhibited specificity for their respective targets, as well as conserved sequence and secondary structure reminiscent of naturally occurring, cis-acting mRNA elements.

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Section: Ugaafaauuaaacaugmentioning

confidence: 99%

High-Affinity RNA Ligands to Escherichia coli Ribosomes and Ribosomal Protein S1: Comparison of Natural and Unnatural Binding Sites

Ringquist¹,

Jones²,

Snyder³

et al. 1995

Biochemistry

116

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“…The turnover numbers for RegB calculated from these reactions are very low compared with other protein enzymes (Ruckman et al, 1995;this work). Clone 25, which is the fastest cleaving ligand so far tested as a substrate for RegB, produces a turnover number of 7.8/min.…”

Section: Discussionmentioning

confidence: 86%

“…Other Proteins. RegB was used for a stock prepared previously (Ruckman et al, 1995). Purified S1 was generously provided by Alap Subramanian of the Max Planck Institute, Berlin, Germany.…”

Section: Methodsmentioning

confidence: 99%

“…The reason for this bias is not clear. Purified preparations of RegB have low rates of cleavage in Vitro compared to its activity in ViVo (Ruckman et al, 1995). However, the activity of RegB in Vitro is enhanced by 1-2 orders of magnitude by ribosomal particles.…”

mentioning

confidence: 97%

“…However, the activity of RegB in Vitro is enhanced by 1-2 orders of magnitude by ribosomal particles. The stimulatory effect is entirely contributed by S1 protein in the 30S particles (Ruckman et al, 1995). Whether S1 mediates this effect through protein-protein interactions with RegB or by interacting with the RNA is not known.…”

mentioning

confidence: 99%

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In Vitro Selection of RNA Specifically Cleaved by Bacteriophage T4 RegB Endonuclease

et al. 1996

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T4 RegB endonuclease specifically cleaves at -GGAG- sites in several early T4 messages, rendering them nonfunctional. Not all -GGAG- sites are processed equally by RegB; those found at the Shine-Dalgarno sequences and in intercistronic regions are processed with higher efficiency than the -GGAG- sites located in coding regions. The low activity of RegB observed in vitro is enhanced by 1-2 orders of magnitude by the Escherichia coli ribosomal protein S1. We have used SELEX (systematic evolution of ligands by exponential enrichment) on a combinatorial RNA library to obtain molecules that are specifically cleaved by T4 RegB endonuclease in the presence of S1. The sequences obtained contain the required -GGAG- tetranucleotide and were unusually enriched in adenosine and cytosine nucleotides. No consensus structure or sequence motif other than -GGAG- was conserved among the selected molecules. The majority of the RNAs are entirely dependent on S1 for RegB-catalyzed cleavage; however, a few RNAs are found to be S1 independent but are cleaved by RegB with much lower rates.

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Endoribonuclease RegB from bacteriophage T4 is necessary for the degradation of early but not middle or late mRNAs11Edited by M. Yaniv

Sanson

Troitskaya

et al. 2000

Journal of Molecular Biology

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The bacteriophage T4 regB ribonuclease. Stimulation of the purified enzyme by ribosomal protein S1.

Cited by 46 publications

References 42 publications

High-Affinity RNA Ligands to Escherichia coli Ribosomes and Ribosomal Protein S1: Comparison of Natural and Unnatural Binding Sites

High-Affinity RNA Ligands to Escherichia coli Ribosomes and Ribosomal Protein S1: Comparison of Natural and Unnatural Binding Sites

In Vitro Selection of RNA Specifically Cleaved by Bacteriophage T4 RegB Endonuclease

Endoribonuclease RegB from bacteriophage T4 is necessary for the degradation of early but not middle or late mRNAs11Edited by M. Yaniv

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