mismatched DNA binding / negative regulation of DNA recombination / ATP-dependent DNA damage sensor activity / mismatch repair / large ribosomal subunit / transferase activity / ribosomal small subunit assembly / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding ...mismatched DNA binding / negative regulation of DNA recombination / ATP-dependent DNA damage sensor activity / mismatch repair / large ribosomal subunit / transferase activity / ribosomal small subunit assembly / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / endonuclease activity / cytosolic large ribosomal subunit / cytoplasmic translation / Hydrolases; Acting on ester bonds / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / ATP hydrolysis activity / RNA binding / zinc ion binding / ATP binding / metal ion binding / cytosol / cytoplasm Similarity search - Function
Endonuclease MutS2 / MutS2 and Smr-associated SH3 domain / MutS2 and Smr-associated SH3 domain / Smr domain / Small MutS-related domain / Smr domain superfamily / Smr domain / Smr domain profile. / DNA mismatch repair MutS family / DNA mismatch repair protein MutS, C-terminal ...Endonuclease MutS2 / MutS2 and Smr-associated SH3 domain / MutS2 and Smr-associated SH3 domain / Smr domain / Small MutS-related domain / Smr domain superfamily / Smr domain / Smr domain profile. / DNA mismatch repair MutS family / DNA mismatch repair protein MutS, C-terminal / DNA mismatch repair protein MutS, core / DNA mismatch repair protein MutS, core domain superfamily / MutS domain V / DNA mismatch repair proteins mutS family signature. / DNA-binding domain of DNA mismatch repair MUTS family / ATPase domain of DNA mismatch repair MUTS family / Type-1 KH domain profile. / : / Ribosomal protein S14, type Z / Ribosomal protein L31 type A / Ribosomal protein S16, conserved site / Ribosomal protein S16 signature. / Ribosomal protein L31 signature. / Ribosomal protein L31 / Ribosomal protein L31 superfamily / Ribosomal protein L31 / Ribosomal protein L16 signature 1. / Ribosomal protein L21, conserved site / Ribosomal protein L21 signature. / Ribosomal protein L16, conserved site / Ribosomal protein L16 signature 2. / Ribosomal protein L6, conserved site / Ribosomal protein L6 signature 1. / : / Ribosomal protein L17 signature. / Ribosomal protein L36 signature. / Ribosomal protein L28/L24 superfamily / Ribosomal protein L32p, bacterial type / Ribosomal protein L33, conserved site / Ribosomal protein L33 signature. / Ribosomal protein L35, conserved site / Ribosomal protein L35 signature. / : / Ribosomal protein L28 / Ribosomal protein L35, non-mitochondrial / Ribosomal protein L5, bacterial-type / Ribosomal protein L18, bacterial-type / : / Ribosomal protein L6, bacterial-type / Ribosomal protein S3, bacterial-type / Ribosomal protein S19, bacterial-type / Ribosomal protein S13, bacterial-type / Ribosomal protein S6, conserved site / Ribosomal protein S6 signature. / Ribosomal protein S14/S29 / Ribosomal protein S7, bacterial/organellar-type / Ribosomal protein S9, bacterial/plastid / Ribosomal protein L36 / Ribosomal protein L36 superfamily / Ribosomal protein L36 / Ribosomal protein S11, bacterial-type / Ribosomal protein S20 / Ribosomal protein S20 superfamily / Ribosomal protein S20 / Ribosomal protein S4, bacterial-type / Ribosomal protein L19, conserved site / Ribosomal protein L19 signature. / 30S ribosomal protein S17 / Ribosomal protein S5, bacterial-type / Ribosomal protein L27, conserved site / Ribosomal protein L27 signature. / Ribosomal protein S6, plastid/chloroplast / Ribosomal protein L20 signature. / Ribosomal protein L22, bacterial/chloroplast-type / Ribosomal protein L14P, bacterial-type / Ribosomal protein L34, conserved site / Ribosomal protein L34 signature. / Ribosomal protein S2, bacteria/mitochondria/plastid / Ribosomal protein L2, bacterial/organellar-type / Ribosomal protein L35 / Ribosomal protein L35 superfamily / Ribosomal protein L35 / Ribosomal protein L33 / Ribosomal protein L33 / Ribosomal L28 family / Ribosomal protein L33 superfamily / Ribosomal protein L16 / Ribosomal protein L28/L24 / Ribosomal protein L18 / Ribosomal L18 of archaea, bacteria, mitoch. and chloroplast / Ribosomal protein S18, conserved site / Ribosomal protein S18 signature. / Ribosomal protein L30, bacterial-type / Ribosomal protein S16 / Ribosomal protein S16 domain superfamily / Ribosomal protein S16 / : / L28p-like / Ribosomal protein S15, bacterial-type / Ribosomal protein S6 Similarity search - Domain/homology
Small ribosomal subunit protein uS7 / Large ribosomal subunit protein uL3 / Large ribosomal subunit protein uL14 / Small ribosomal subunit protein uS13 / Large ribosomal subunit protein uL4 / Large ribosomal subunit protein uL23 / Large ribosomal subunit protein uL16 / Large ribosomal subunit protein uL5 / Large ribosomal subunit protein uL2 / Large ribosomal subunit protein bL17 ...Small ribosomal subunit protein uS7 / Large ribosomal subunit protein uL3 / Large ribosomal subunit protein uL14 / Small ribosomal subunit protein uS13 / Large ribosomal subunit protein uL4 / Large ribosomal subunit protein uL23 / Large ribosomal subunit protein uL16 / Large ribosomal subunit protein uL5 / Large ribosomal subunit protein uL2 / Large ribosomal subunit protein bL17 / Large ribosomal subunit protein uL13 / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein uS17 / Small ribosomal subunit protein uS8 / Large ribosomal subunit protein uL15 / Small ribosomal subunit protein uS9 / Large ribosomal subunit protein bL34 / Small ribosomal subunit protein bS6 / Large ribosomal subunit protein bL31 / Small ribosomal subunit protein uS4 / Large ribosomal subunit protein bL27 / Small ribosomal subunit protein uS2 / Large ribosomal subunit protein bL20 / Large ribosomal subunit protein bL35 / Large ribosomal subunit protein bL28 / Small ribosomal subunit protein bS16 / Large ribosomal subunit protein bL19 / Large ribosomal subunit protein bL21 / Small ribosomal subunit protein bS20 / Large ribosomal subunit protein bL36 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein uS15 / Large ribosomal subunit protein bL33 / Small ribosomal subunit protein bS18 / Large ribosomal subunit protein bL32 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein uS11 / Large ribosomal subunit protein uL6 / Endonuclease MutS2 / Large ribosomal subunit protein uL24 / Large ribosomal subunit protein uL18 / Large ribosomal subunit protein uL22 / Small ribosomal subunit protein uS19 / Large ribosomal subunit protein uL30 / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS10 / Large ribosomal subunit protein uL29 Similarity search - Component
Biological species
Bacillus subtilis (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 3.57 Å
Journal: EMBO J / Year: 2024 Title: B. subtilis MutS2 splits stalled ribosomes into subunits without mRNA cleavage. Authors: Esther N Park / Timur Mackens-Kiani / Rebekah Berhane / Hanna Esser / Chimeg Erdenebat / A Maxwell Burroughs / Otto Berninghausen / L Aravind / Roland Beckmann / Rachel Green / Allen R Buskirk / Abstract: Stalled ribosomes are rescued by pathways that recycle the ribosome and target the nascent polypeptide for degradation. In E. coli, these pathways are triggered by ribosome collisions through the ...Stalled ribosomes are rescued by pathways that recycle the ribosome and target the nascent polypeptide for degradation. In E. coli, these pathways are triggered by ribosome collisions through the recruitment of SmrB, a nuclease that cleaves the mRNA. In B. subtilis, the related protein MutS2 was recently implicated in ribosome rescue. Here we show that MutS2 is recruited to collisions by its SMR and KOW domains, and we reveal the interaction of these domains with collided ribosomes by cryo-EM. Using a combination of in vivo and in vitro approaches, we show that MutS2 uses its ABC ATPase activity to split ribosomes, targeting the nascent peptide for degradation through the ribosome quality control pathway. However, unlike SmrB, which cleaves mRNA in E. coli, we see no evidence that MutS2 mediates mRNA cleavage or promotes ribosome rescue by tmRNA. These findings clarify the biochemical and cellular roles of MutS2 in ribosome rescue in B. subtilis and raise questions about how these pathways function differently in diverse bacteria.
Entire : MutS2-disome complex from B. subtilis, focus refined, collided 70S
Entire
Name: MutS2-disome complex from B. subtilis, focus refined, collided 70S
Components
Complex: MutS2-disome complex from B. subtilis, focus refined, collided 70S
Complex: B. subtilis Endonuclease MutS2 binding the collided ribosome interface
Protein or peptide: Endonuclease MutS2
Protein or peptide: 50S ribosomal protein L32
Protein or peptide: Large ribosomal subunit protein bL33
Protein or peptide: Large ribosomal subunit protein bL34
Protein or peptide: Large ribosomal subunit protein bL35
Protein or peptide: 50S ribosomal protein L36
Protein or peptide: Large ribosomal subunit protein bL31
RNA: 16S rRNA (1533-MER)
Protein or peptide: 30S ribosomal protein S2
Protein or peptide: 30S ribosomal protein S3
Protein or peptide: 30S ribosomal protein S4
Protein or peptide: 30S ribosomal protein S5
Protein or peptide: 30S ribosomal protein S6
Protein or peptide: 30S ribosomal protein S7
Protein or peptide: 30S ribosomal protein S8
Protein or peptide: 30S ribosomal protein S9
Protein or peptide: 30S ribosomal protein S10
Protein or peptide: 30S ribosomal protein S11
Protein or peptide: 30S ribosomal protein S12
Protein or peptide: 30S ribosomal protein S13
Protein or peptide: 30S ribosomal protein S14 type Z
Protein or peptide: 30S ribosomal protein S15
Protein or peptide: 30S ribosomal protein S16
Protein or peptide: 30S ribosomal protein S17
Protein or peptide: 30S ribosomal protein S18
Protein or peptide: 30S ribosomal protein S19
Protein or peptide: 30S ribosomal protein S20
RNA: tRNA (77-MER)
RNA: 5S rRNA (112-MER)
Protein or peptide: Large ribosomal subunit protein uL2
Protein or peptide: Large ribosomal subunit protein uL3
Protein or peptide: Large ribosomal subunit protein uL4
Protein or peptide: Large ribosomal subunit protein uL5
Protein or peptide: Large ribosomal subunit protein uL6
Protein or peptide: Large ribosomal subunit protein uL13
Protein or peptide: 50S ribosomal protein L14
Protein or peptide: 50S ribosomal protein L15
Protein or peptide: Large ribosomal subunit protein uL16
Protein or peptide: Large ribosomal subunit protein bL17
Protein or peptide: 50S ribosomal protein L18
Protein or peptide: 50S ribosomal protein L19
Protein or peptide: Large ribosomal subunit protein bL20
Protein or peptide: Large ribosomal subunit protein bL21
Protein or peptide: Large ribosomal subunit protein uL22
Protein or peptide: Large ribosomal subunit protein uL23
Protein or peptide: Large ribosomal subunit protein uL24
Protein or peptide: Large ribosomal subunit protein bL27
Protein or peptide: Large ribosomal subunit protein bL28
Protein or peptide: Large ribosomal subunit protein uL29
Protein or peptide: Large ribosomal subunit protein uL30
RNA: 23S RNA (2887-MER)
RNA: mRNA (33-MER)
RNA: tRNA (73-MER)
+
Supramolecule #1: MutS2-disome complex from B. subtilis, focus refined, collided 70S
Supramolecule
Name: MutS2-disome complex from B. subtilis, focus refined, collided 70S type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#6, #8-#28, #30-#52, #29, #53, #7 Details: Collided ribosomes from B. subtilis (purified from natural source) reconstituted with recombinantly expressed and purified B. subtilis MutS2. Focus refined reconstruction, with a mask ...Details: Collided ribosomes from B. subtilis (purified from natural source) reconstituted with recombinantly expressed and purified B. subtilis MutS2. Focus refined reconstruction, with a mask covering the collided ribosome and MutS2.
Source (natural)
Organism: Bacillus subtilis (bacteria)
+
Supramolecule #2: B. subtilis Endonuclease MutS2 binding the collided ribosome interface
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