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TitleMolecular basis for cA6 synthesis by a type III-A CRISPR-Cas enzyme and its conversion to cA4 production.
Journal, issue, pagesNucleic Acids Res, Year 2024
Publish dateJul 11, 2024
AuthorsHemant N Goswami / Fozieh Ahmadizadeh / Bing Wang / Doreen Addo-Yobo / Yu Zhao / A Carl Whittington / Huan He / Michael P Terns / Hong Li /
PubMed AbstractThe type III-A (Csm) CRISPR-Cas systems are multi-subunit and multipronged prokaryotic enzymes in guarding the hosts against viral invaders. Beyond cleaving activator RNA transcripts, Csm confers ...The type III-A (Csm) CRISPR-Cas systems are multi-subunit and multipronged prokaryotic enzymes in guarding the hosts against viral invaders. Beyond cleaving activator RNA transcripts, Csm confers two additional activities: shredding single-stranded DNA and synthesizing cyclic oligoadenylates (cOAs) by the Cas10 subunit. Known Cas10 enzymes exhibit a fascinating diversity in cOA production. Three major forms-cA3, cA4 and cA6have been identified, each with the potential to trigger unique downstream effects. Whereas the mechanism for cOA-dependent activation is well characterized, the molecular basis for synthesizing different cOA isoforms remains unclear. Here, we present structural characterization of a cA6-producing Csm complex during its activation by an activator RNA. Analysis of the captured intermediates of cA6 synthesis suggests a 3'-to-5' nucleotidyl transferring process. Three primary adenine binding sites can be identified along the chain elongation path, including a unique tyrosine-threonine dyad found only in the cA6-producing Cas10. Consistently, disrupting the tyrosine-threonine dyad specifically impaired cA6 production while promoting cA4 production. These findings suggest that Cas10 utilizes a unique enzymatic mechanism for forming the phosphodiester bond and has evolved distinct strategies to regulate the cOA chain length.
External linksNucleic Acids Res / PubMed:38989619
MethodsEM (single particle)
Resolution2.58 - 2.79 Å
Structure data

43814
EMDB entry, No image

9ash

EMDB-43814, PDB-9ash:
Cryo-EM structure of the active Lactococcus lactis Csm bound to target in post-cleavage stage
Method: EM (single particle) / Resolution: 2.58 Å

43815
EMDB entry, No image

9asi

EMDB-43815, PDB-9asi:
Cryo-EM structure of the active Lactococcus lactis Csm bound to target in pre-cleavage stage
Method: EM (single particle) / Resolution: 2.79 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • lactococcus lactis subsp. lactis (lactic acid bacteria)
KeywordsRNA BINDING PROTEIN/RNA / Type III-A CRISPR-Cas / Csm / Cyclic Oligoadenylate synthesis / RNA BINDING PROTEIN-RNA complex

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