Activation of the RegB endoribonuclease by the S1 ribosomal protein is due to cooperation between the S1 four C-terminal modules in a substrate-dependant manner.
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Probing the relationship between Gram-negative and Gram-positive S1 proteins by sequence analysisResonance assignment of the ribosome binding domain of E. coli ribosomal protein S1Rrp5p, a trans-acting factor in yeast ribosome biogenesis, is an RNA-binding protein with a pronounced preference for U-rich sequences.Protein aggregation in a mutant deficient in yajL, the bacterial homolog of the Parkinsonism-associated protein DJ-1The deleterious effect of an insertion sequence removing the last twenty percent of the essential Escherichia coli rpsA gene is due to mRNA destabilization, not protein truncationRibosomal protein S1 binds mRNA and tmRNA similarly but plays distinct roles in translation of these moleculesPost-transcriptional control by bacteriophage T4: mRNA decay and inhibition of translation initiation.The sequences and activities of RegB endoribonucleases of T4-related bacteriophages.Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11 nt conserved sequence.S1 ribosomal protein functions in translation initiation and ribonuclease RegB activation are mediated by similar RNA-protein interactions: an NMR and SAXS analysis.
P2860
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P2860
Activation of the RegB endoribonuclease by the S1 ribosomal protein is due to cooperation between the S1 four C-terminal modules in a substrate-dependant manner.
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name
Activation of the RegB endorib ...... a substrate-dependant manner.
@en
Activation of the RegB endorib ...... a substrate-dependant manner.
@nl
type
label
Activation of the RegB endorib ...... a substrate-dependant manner.
@en
Activation of the RegB endorib ...... a substrate-dependant manner.
@nl
prefLabel
Activation of the RegB endorib ...... a substrate-dependant manner.
@en
Activation of the RegB endorib ...... a substrate-dependant manner.
@nl
P2093
P2860
P356
P1476
Activation of the RegB endorib ...... a substrate-dependant manner.
@en
P2093
Francois Bontems
Marco Bisaglia
Soumaya Laalami
P2860
P304
15261-15271
P356
10.1074/JBC.M212731200
P407
P577
2003-02-07T00:00:00Z