7PZE

MademoiseLLE domain 2 of Rrm4 from Ustilago maydis

Summary for 7PZE

• Entry DOI: 10.2210/pdb7pze/pdb
• Descriptor: Chromosome 8, whole genome shotgun sequence (1 entity in total)
• Functional Keywords: endosome / pam2 / poly(a)-binding protein / rna transport / ustilago maydis, rna binding protein
• Biological source: Ustilago maydis
• Total number of polymer chains: 2
• Total formula weight: 80766.76

Authors

Devans, S.,Schott-Verdugo, s.,Muentjes, K.,Olgeiser, L.,Reiners, J.,Schmitt, L.,Hoeppner, A.,Smits, S.H.,Gohlke, H.,Feldbruegge, M. (deposition date: 2021-10-12, release date: 2022-06-15, Last modification date: 2024-05-01)

Primary citation

Devan, S.K.,Schott-Verdugo, S.,Muntjes, K.,Bismar, L.,Reiners, J.,Hachani, E.,Schmitt, L.,Hoppner, A.,Smits, S.H.,Gohlke, H.,Feldbrugge, M.
A MademoiseLLE domain binding platform links the key RNA transporter to endosomes.
Plos Genet., 18:e1010269-e1010269, 2022

PubMed Abstract: Spatiotemporal expression can be achieved by transport and translation of mRNAs at defined subcellular sites. An emerging mechanism mediating mRNA trafficking is microtubule-dependent co-transport on shuttling endosomes. Although progress has been made in identifying various components of the endosomal mRNA transport machinery, a mechanistic understanding of how these RNA-binding proteins are connected to endosomes is still lacking. Here, we demonstrate that a flexible MademoiseLLE (MLLE) domain platform within RNA-binding protein Rrm4 of Ustilago maydis is crucial for endosomal attachment. Our structure/function analysis uncovered three MLLE domains at the C-terminus of Rrm4 with a functionally defined hierarchy. MLLE3 recognises two PAM2-like sequences of the adaptor protein Upa1 and is essential for endosomal shuttling of Rrm4. MLLE1 and MLLE2 are most likely accessory domains exhibiting a variable binding mode for interaction with currently unknown partners. Thus, endosomal attachment of the mRNA transporter is orchestrated by a sophisticated MLLE domain binding platform.

PubMed: 35727840
DOI: 10.1371/journal.pgen.1010269

Experimental method

X-RAY DIFFRACTION (2.6 Å)