The La-related protein 1-specific domain repurposes HEAT-like repeats to directly bind a 5'TOP sequence

Lahr, Roni M.; Mack, Seshat M.; Heroux, Annie; Blagden, Sarah P.; Bousquet-Antonelli, Cecile; Deragon, Jean -Marc; Berman, Andrea J.

doi:10.1093/nar/gkv748

Title: The La-related protein 1-specific domain repurposes HEAT-like repeats to directly bind a 5'TOP sequence

Journal Article · Wed Jul 22 00:00:00 EDT 2015 · Nucleic Acids Research

DOI:https://doi.org/10.1093/nar/gkv748· OSTI ID:1229454

Lahr, Roni M. ^[1]; Mack, Seshat M. ^[1]; Heroux, Annie ^[2]; Blagden, Sarah P. ^[3]; Bousquet-Antonelli, Cecile ^[4]; Deragon, Jean -Marc ^[4]; Berman, Andrea J. ^[1]

Univ. of Pittsburgh, Pittsburgh, PA (United States)
Brookhaven National Lab. (BNL), Upton, NY (United States)
Univ. of Oxford, Oxford (United Kingdom)
CNRS-UMR5096, Perpignan (France); Univ. de Perpignan-UMR5096, Perpignan (France)

La-related protein 1 (LARP1) regulates the stability of many mRNAs. These include 5'TOPs, mTOR-kinase responsive mRNAs with pyrimidine-rich 5' UTRs, which encode ribosomal proteins and translation factors. We determined that the highly conserved LARP1-specific C-terminal DM15 region of human LARP1 directly binds a 5'TOP sequence. The crystal structure of this DM15 region refined to 1.86 Å resolution has three structurally related and evolutionarily conserved helix-turn-helix modules within each monomer. These motifs resemble HEAT repeats, ubiquitous helical protein-binding structures, but their sequences are inconsistent with consensus sequences of known HEAT modules, suggesting this structure has been repurposed for RNA interactions. A putative mTORC1-recognition sequence sits within a flexible loop C-terminal to these repeats. We also present modelling of pyrimidine-rich single-stranded RNA onto the highly conserved surface of the DM15 region. Ultimately, these studies lay the foundation necessary for proceeding toward a structural mechanism by which LARP1 links mTOR signalling to ribosome biogenesis.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC00112704; AC02-98CH10886; FWP BO-70; MWRIF 8059; 8P41GM103473-16

OSTI ID:: 1229454

Report Number(s):: BNL-111530-2015-JA

Journal Information:: Nucleic Acids Research, Vol. 43, Issue 16; ISSN 0305-1048

Publisher:: Oxford University PressCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 41 works

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