Capturing the Mechanism Underlying TOP mRNA Binding to LARP1.

ABSTRACT: The RNA-binding protein La-related protein 1 (LARP1) plays a central role in ribosome biosynthesis. Its C-terminal DM15 region binds the 7-methylguanosine (m⁷G) cap and 5' terminal oligopyrimidine (TOP) motif characteristic of transcripts encoding ribosomal proteins and translation factors. Under the control of mammalian target of rapamycin complex 1 (mTORC1), LARP1 regulates translation of these transcripts. Characterizing the dynamics of DM15-TOP recognition is essential to understanding this fundamental biological process. We use molecular dynamics simulations, biophysical assays, and X-ray crystallography to reveal the mechanism of DM15 binding to TOP transcripts. Residues C-terminal to the m⁷G-binding site play important roles in cap recognition. Furthermore, we

SUBMITTER: Cassidy KC 

PROVIDER: S-EPMC7269035 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature