Summary information and primary citation
- PDB-id
-
7oi8;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ribosome
- Method
- cryo-EM (3.5 Å)
- Summary
- cryo-EM structure of late human 39s mitoribosome
assembly intermediates, state 3a
- Reference
-
Cheng J, Berninghausen O, Beckmann R (2021): "A distinct
assembly pathway of the human 39S late
pre-mitoribosome." Nat Commun,
12, 4544. doi: 10.1038/s41467-021-24818-x.
- Abstract
- Assembly of the mitoribosome is largely enigmatic and
involves numerous assembly factors. Little is known about
their function and the architectural transitions of the
pre-ribosomal intermediates. Here, we solve cryo-EM
structures of the human 39S large subunit pre-ribosomes,
representing five distinct late states. Besides the MALSU1
complex used as bait for affinity purification, we identify
several assembly factors, including the DDX28 helicase,
MRM3, GTPBP10 and the NSUN4-mTERF4 complex, all of which
keep the 16S rRNA in immature conformations. The late
transitions mainly involve rRNA domains IV and V, which
form the central protuberance, the intersubunit side and
the peptidyltransferase center of the 39S subunit.
Unexpectedly, we find deacylated tRNA in the ribosomal
E-site, suggesting a role in 39S assembly. Taken together,
our study provides an architectural inventory of the
distinct late assembly phase of the human 39S
mitoribosome.