6RO1

X-ray crystal structure of the MTR4 NVL complex

Summary for 6RO1

• Entry DOI: 10.2210/pdb6ro1/pdb
• Descriptor: Exosome RNA helicase MTR4, Nuclear valosin-containing protein-like, SULFATE ION, ... (6 entities in total)
• Functional Keywords: dexh helicase, complex, rna binding protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 117653.42

Authors

Lingaraju, M.,Langer, L.M.,Basquin, J.,Falk, S.,Conti, E. (deposition date: 2019-05-10, release date: 2019-07-03, Last modification date: 2024-01-24)

Primary citation

Lingaraju, M.,Johnsen, D.,Schlundt, A.,Langer, L.M.,Basquin, J.,Sattler, M.,Heick Jensen, T.,Falk, S.,Conti, E.
The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs.
Nat Commun, 10:3393-3393, 2019

PubMed Abstract: The nuclear exosome and its essential co-factor, the RNA helicase MTR4, play crucial roles in several RNA degradation pathways. Besides unwinding RNA substrates for exosome-mediated degradation, MTR4 associates with RNA-binding proteins that function as adaptors in different RNA processing and decay pathways. Here, we identify and characterize the interactions of human MTR4 with a ribosome processing adaptor, NVL, and with ZCCHC8, an adaptor involved in the decay of small nuclear RNAs. We show that the unstructured regions of NVL and ZCCHC8 contain short linear motifs that bind the MTR4 arch domain in a mutually exclusive manner. These short sequences diverged from the arch-interacting motif (AIM) of yeast rRNA processing factors. Our results suggest that nuclear exosome adaptors have evolved canonical and non-canonical AIM sequences to target human MTR4 and demonstrate the versatility and specificity with which the MTR4 arch domain can recruit a repertoire of different RNA-binding proteins.

PubMed: 31358741
DOI: 10.1038/s41467-019-11339-x

Experimental method

X-RAY DIFFRACTION (3.07 Å)