6T59

Structure of rabbit 80S ribosome translating beta-tubulin in complex with tetratricopeptide protein 5 and nascent chain-associated complex

This is a non-PDB format compatible entry.

Summary for 6T59

• Entry DOI: 10.2210/pdb6t59/pdb
• EMDB information: 10380
• Descriptor: Ribosomal protein L8, Ribosomal protein L11, eL13, ... (55 entities in total)
• Functional Keywords: tubulin, nascent chain-associated complex, ribosome-nascent chain, tetratricopeptide protein 5, autoregulation, ribosome
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 53
• Total formula weight: 2262178.98

Authors

Lin, Z.,Gasic, I.,Chandrasekaran, V.,Peters, N.,Shao, S.,Ramakrishnan, V.,Mitchison, T.J.,Hegde, R.S. (deposition date: 2019-10-15, release date: 2019-11-27, Last modification date: 2020-01-15)

Primary citation

Lin, Z.,Gasic, I.,Chandrasekaran, V.,Peters, N.,Shao, S.,Mitchison, T.J.,Hegde, R.S.
TTC5 mediates autoregulation of tubulin via mRNA degradation.
Science, 367:100-104, 2020

PubMed Abstract: Tubulins play crucial roles in cell division, intracellular traffic, and cell shape. Tubulin concentration is autoregulated by feedback control of messenger RNA (mRNA) degradation via an unknown mechanism. We identified tetratricopeptide protein 5 (TTC5) as a tubulin-specific ribosome-associating factor that triggers cotranslational degradation of tubulin mRNAs in response to excess soluble tubulin. Structural analysis revealed that TTC5 binds near the ribosome exit tunnel and engages the amino terminus of nascent tubulins. TTC5 mutants incapable of ribosome or nascent tubulin interaction abolished tubulin autoregulation and showed chromosome segregation defects during mitosis. Our findings show how a subset of mRNAs can be targeted for coordinated degradation by a specificity factor that recognizes the nascent polypeptides they encode.

PubMed: 31727855
DOI: 10.1126/science.aaz4352

Experimental method

ELECTRON MICROSCOPY (3.11 Å)