8Q66

Crystal Structure of the C. elegans MUT-7 MUT-8 CTD complex

Summary for 8Q66

• Entry DOI: 10.2210/pdb8q66/pdb
• Descriptor: Exonuclease mut-7, SH2 domain-containing protein, ZINC ION, ... (5 entities in total)
• Functional Keywords: small rna amplification mutator complex exoribonuclease, rna binding protein
• Biological source: Caenorhabditis elegans; More
• Total number of polymer chains: 2
• Total formula weight: 60425.66

Authors

Falk, S.,Busetto, V. (deposition date: 2023-08-11, release date: 2024-03-06, Last modification date: 2024-09-18)

Primary citation

Busetto, V.,Pshanichnaya, L.,Lichtenberger, R.,Hann, S.,Ketting, R.F.,Falk, S.
MUT-7 exoribonuclease activity and localization are mediated by an ancient domain.
Nucleic Acids Res., 52:9076-9091, 2024

PubMed Abstract: The MUT-7 family of 3'-5' exoribonucleases is evolutionarily conserved across the animal kingdom and plays essential roles in small RNA production in the germline. Most MUT-7 homologues carry a C-terminal domain of unknown function named MUT7-C appended to the exoribonuclease domain. Our analysis shows that the MUT7-C is evolutionary ancient, as a minimal version of the domain exists as an individual protein in prokaryotes. In animals, MUT7-C has acquired an insertion that diverged during evolution, expanding its functions. Caenorhabditis elegans MUT-7 contains a specific insertion within MUT7-C, which allows binding to MUT-8 and, consequently, MUT-7 recruitment to germ granules. In addition, in C. elegans and human MUT-7, the MUT7-C domain contributes to RNA binding and is thereby crucial for ribonuclease activity. This RNA-binding function most likely represents the ancestral function of the MUT7-C domain. Overall, this study sheds light on MUT7-C and assigns two functions to this previously uncharacterized domain.

PubMed: 39188014
DOI: 10.1093/nar/gkae610

Experimental method

X-RAY DIFFRACTION (2.03 Å)