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!align=left |Citation | |||
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'''Gagnon, MG, Seetharaman, SV, Bulkley, D and Steitz, TA''' (2012) Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome.''Science'' '''335''':1370-2 | |||
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!align=left |Abstract | |||
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In bacteria, the hybrid transfer-messenger RNA (tmRNA) rescues ribosomes stalled on defective messenger RNAs (mRNAs). However, certain gram-negative bacteria have evolved proteins that are capable of rescuing stalled ribosomes in a tmRNA-independent manner. Here, we report a 3.2 angstrom-resolution crystal structure of the rescue factor YaeJ bound to the Thermus thermophilus 70S ribosome in complex with the initiator tRNA(i)(fMet) and a short mRNA. The structure reveals that the C-terminal tail of YaeJ functions as a sensor to discriminate between stalled and actively translating ribosomes by binding in the mRNA entry channel downstream of the A site between the head and shoulder of the 30S subunit. This allows the N-terminal globular domain to sample different conformations, so that its conserved GGQ motif is optimally positioned to catalyze the hydrolysis of peptidyl-tRNA. This structure gives insights into the mechanism of YaeJ function and provides a basis for understanding how it rescues stalled ribosomes. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=22422986 PubMed] | |||
Online version:[http://dx.doi.org/10.1126/science.1217443 10.1126/science.1217443] | |||
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!align=left |Keywords | |||
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Amino Acid Sequence; Carboxylic Ester Hydrolases; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Protein Biosynthesis; Protein Structure, Tertiary; RNA, Bacterial; RNA, Messenger; RNA, Ribosomal; RNA, Transfer, Amino Acyl; RNA, Transfer, Met; Ribosome Subunits, Large, Bacterial; Ribosome Subunits, Small, Bacterial; Ribosomes; Thermus thermophilus | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
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== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
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==Annotations {{HelpIcon|Help:Literature}}== | |||
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | |||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
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Revision as of 22:09, 11 April 2012
| Citation |
Gagnon, MG, Seetharaman, SV, Bulkley, D and Steitz, TA (2012) Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome.Science 335:1370-2 |
|---|---|
| Abstract |
In bacteria, the hybrid transfer-messenger RNA (tmRNA) rescues ribosomes stalled on defective messenger RNAs (mRNAs). However, certain gram-negative bacteria have evolved proteins that are capable of rescuing stalled ribosomes in a tmRNA-independent manner. Here, we report a 3.2 angstrom-resolution crystal structure of the rescue factor YaeJ bound to the Thermus thermophilus 70S ribosome in complex with the initiator tRNA(i)(fMet) and a short mRNA. The structure reveals that the C-terminal tail of YaeJ functions as a sensor to discriminate between stalled and actively translating ribosomes by binding in the mRNA entry channel downstream of the A site between the head and shoulder of the 30S subunit. This allows the N-terminal globular domain to sample different conformations, so that its conserved GGQ motif is optimally positioned to catalyze the hydrolysis of peptidyl-tRNA. This structure gives insights into the mechanism of YaeJ function and provides a basis for understanding how it rescues stalled ribosomes. |
| Links |
PubMed Online version:10.1126/science.1217443 |
| Keywords |
Amino Acid Sequence; Carboxylic Ester Hydrolases; Crystallography, X-Ray; Escherichia coli; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Protein Biosynthesis; Protein Structure, Tertiary; RNA, Bacterial; RNA, Messenger; RNA, Ribosomal; RNA, Transfer, Amino Acyl; RNA, Transfer, Met; Ribosome Subunits, Large, Bacterial; Ribosome Subunits, Small, Bacterial; Ribosomes; Thermus thermophilus |
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