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TitleBacterial ribosome collision sensing by a MutS DNA repair ATPase paralogue.
Journal, issue, pagesNature, Vol. 603, Issue 7901, Page 509-514, Year 2022
Publish dateMar 9, 2022
AuthorsFederico Cerullo / Sebastian Filbeck / Pratik Rajendra Patil / Hao-Chih Hung / Haifei Xu / Julia Vornberger / Florian W Hofer / Jaro Schmitt / Guenter Kramer / Bernd Bukau / Kay Hofmann / Stefan Pfeffer / Claudio A P Joazeiro /
PubMed AbstractRibosome stalling during translation is detrimental to cellular fitness, but how this is sensed and elicits recycling of ribosomal subunits and quality control of associated mRNA and incomplete ...Ribosome stalling during translation is detrimental to cellular fitness, but how this is sensed and elicits recycling of ribosomal subunits and quality control of associated mRNA and incomplete nascent chains is poorly understood. Here we uncover Bacillus subtilis MutS2, a member of the conserved MutS family of ATPases that function in DNA mismatch repair, as an unexpected ribosome-binding protein with an essential function in translational quality control. Cryo-electron microscopy analysis of affinity-purified native complexes shows that MutS2 functions in sensing collisions between stalled and translating ribosomes and suggests how ribosome collisions can serve as platforms to deploy downstream processes: MutS2 has an RNA endonuclease small MutS-related (SMR) domain, as well as an ATPase/clamp domain that is properly positioned to promote ribosomal subunit dissociation, which is a requirement both for ribosome recycling and for initiation of ribosome-associated protein quality control (RQC). Accordingly, MutS2 promotes nascent chain modification with alanine-tail degrons-an early step in RQC-in an ATPase domain-dependent manner. The relevance of these observations is underscored by evidence of strong co-occurrence of MutS2 and RQC genes across bacterial phyla. Overall, the findings demonstrate a deeply conserved role for ribosome collisions in mounting a complex response to the interruption of translation within open reading frames.
External linksNature / PubMed:35264791 / PubMed Central
MethodsEM (single particle)
Resolution3.21 - 5.68 Å
Structure data

EMDB-14156:
Cryo-EM reconstruction of the Bacillus subtilis MutS2-collided disome complex (MutS2 conf.1; Leading 70S)
Method: EM (single particle) / Resolution: 5.68 Å

14157

7qv1

EMDB-14157: Composite reconstruction of the Bacillus subtilis collided disome (Leading 70S)
PDB-7qv1: Bacillus subtilis collided disome (Leading 70S)
Method: EM (single particle) / Resolution: 3.5 Å

14158

7qv2

EMDB-14158: Composite reconstruction of the Bacillus subtilis collided disome (Collided 70S)
PDB-7qv2: Bacillus subtilis collided disome (Collided 70S)
Method: EM (single particle) / Resolution: 3.5 Å

14159

7qv3

EMDB-14159: Cryo-EM reconstruction of the Bacillus subtilis MutS2-collided disome complex (MutS2 conf.2; Leading 70S)
PDB-7qv3: Bacillus subtilis MutS2-collided disome complex (MutS2 conf.2; Leading 70S)
Method: EM (single particle) / Resolution: 5.14 Å

EMDB-14160:
Cryo-EM reconstruction of the Bacillus subtilis MutS2-collided disome complex (Leading 70S)
Method: EM (single particle) / Resolution: 4.22 Å

EMDB-14161:
Cryo-EM reconstruction of the Bacillus subtilis MutS2-collided disome complex (Collided 70S)
Method: EM (single particle) / Resolution: 4.92 Å

EMDB-14162:
Cryo-EM reconstruction of the Bacillus subtilis collided disome (Leading 70S)
Method: EM (single particle) / Resolution: 3.38 Å

EMDB-14163:
Cryo-EM reconstruction of the Bacillus subtilis collided disome (Leading 30S)
Method: EM (single particle) / Resolution: 3.56 Å

EMDB-14164:
Cryo-EM reconstruction of the Bacillus subtilis collided disome (Collided 70S)
Method: EM (single particle) / Resolution: 3.43 Å

EMDB-14165:
Cryo-EM reconstruction of the Bacillus subtilis collided disome (Collided 30S)
Method: EM (single particle) / Resolution: 3.47 Å

EMDB-14166:
Cryo-EM reconstruction of Bacillus subtilis obstructed 50S subunit co-purified with MutS2
Method: EM (single particle) / Resolution: 3.21 Å

Source
  • bacillus subtilis subsp. subtilis str. 168 (bacteria)
KeywordsRIBOSOME / Collision / MutS2 / disome / RQC / ssra / ribosomal collision / mRNA endonuclease

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