Ribosome rearrangements at the onset of translational bypassing

被引：30

作者：

Agirrezabala, Xabier ^{[1
]}

Samatova, Ekaterina ^{[2
]}

Klimova, Mariia ^{[2
]}

Zamora, Miguel ^{[1
]}

Gil-Carton, David ^{[1
]}

Rodnina, Marina V. ^{[2
]}

Valle, Mikel ^{[1
]}

机构：

[1] CIC BioGUNE, Struct Biol Unit, Derio 48160, Spain

[2] Max Planck Inst Biophys Chem, Dept Phys Biochem, D-37077 Gottingen, Germany

来源：

SCIENCE ADVANCES | 2017年 / 3卷 / 06期

关键词：

MESSENGER-RNA STRUCTURE; PEPTIDE-BOND FORMATION; STRUCTURAL BASIS; CRYSTAL-STRUCTURE; MOLECULAR-BASIS; ACTIVE-SITE; CODING GAP; TERMINATION; INSIGHTS; RELEASE;

D O I：

10.1126/sciadv.1700147

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Bypassing is a recoding event that leads to the translation of two distal open reading frames into a single polypeptide chain. We present the structure of a translating ribosome stalled at the bypassing take-off site of gene 60 of bacteriophage T4. The nascent peptide in the exit tunnel anchors the P-site peptidyl-tRNAGly to the ribosome and locks an inactive conformation of the peptidyl transferase center (PTC). The mRNA forms a short dynamic hairpin in the decoding site. The ribosomal subunits adopt a rolling conformation inwhich the rotation of the small subunit around its long axis causes the opening of the A-site region. Together, PTC conformation and mRNA structure safeguard against premature termination and read-through of the stop codon and reconfigure the ribosome to a state poised for take-off and sliding along the noncoding mRNA gap.

引用

页数：8

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