PXD031985 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Conformational rearrangements upon start codon recognition in human 48S translation initiation complex |
Description | Selection of the translation start codon is a key step during protein synthesis in human cells. We obtained cryo-EM structures of human 48S initiation complexes and characterized the intermediates of codon recognition by kinetic methods using eIF1A as a reporter. Both approaches capture two distinct ribosome populations formed on an mRNA with a cognate AUG codon in the presence of eIF1A, eIF1, eIF2–GTP–Met-tRNAiMet, eIF3, eIF4A and eIF4B. The ‘open’ 40S subunit conformation differs from the human 48S scanning complex and represents an intermediate preceding the codon recognition step. The ‘closed’ form is similar to reported structures of complexes from yeast and mammals formed upon codon recognition, except for the orientation of eIF1A, which is unique in our structure. Kinetic experiments show how various initiation factors mediate the population distribution of open and closed conformations until 60S subunit docking. Our results provide insights into the timing and structure of human translation initiation intermediates and suggest the differences in the mechanisms of start codon selection between mammals and yeast. |
HostingRepository | PRIDE |
AnnounceDate | 2022-06-09 |
AnnouncementXML | Submission_2022-06-09_08:59:38.711.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Henning Urlaub |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-03-02 01:10:57 | ID requested | |
⏵ 1 | 2022-06-09 08:59:40 | announced | |
Publication List
Yi SH, Petrychenko V, Schliep JE, Goyal A, Linden A, Chari A, Urlaub H, Stark H, Rodnina MV, Adio S, Fischer N, Conformational rearrangements upon start codon recognition in human 48S translation initiation complex. Nucleic Acids Res, 50(9):5282-5298(2022) [pubmed] |
Keyword List
submitter keyword: Ribosome, 48S initiation comples, eIF1 |
Contact List
Prof. Dr. Henning Urlaub |
contact affiliation | Bioanalytical Mass spectroscopy Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany; Bioanalytics, Institute for Clinical Chemistry, University Medical Center Göttingen, Germany |
contact email | henning.urlaub@mpinat.mpg.de |
lab head | |
Henning Urlaub |
contact affiliation | Max-Plank Institute for Biophysical Chemistry |
contact email | msbio.goettingen@gmail.com |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
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[ - ]
- PRIDE
- PXD031985
- Label: PRIDE project
- Name: Conformational rearrangements upon start codon recognition in human 48S translation initiation complex