Domain definition and interaction mapping for the endonuclease complex hNob1/hPno1

RNA Biol. 2018;15(9):1174-1180. doi: 10.1080/15476286.2018.1517013. Epub 2018 Sep 18.

Abstract

Ribosome biogenesis requires a variety of trans-acting factors in order to produce functional ribosomal subunits. In human cells, the complex formed by the proteins hNob1 and hPno1 is crucial to the site 3 cleavage occurring at the 3'-end of 18S pre-rRNA. However, the properties and activity of this complex are still poorly understood. We present here a detailed characterization of hNob1 organization and its interaction with hPno1. We redefine the boundaries of the endonuclease PIN domain present in hNob1 and we further delineate the precise interacting modules required for complex formation in hNob1 and hPno1. Altogether, our data contributes to a better understanding of the complex biology required during the site 3 cleavage step in ribosome biogenesis.

Keywords: KH domain; PIN domain; Ribosome biogenesis; endonuclease; pre-rRNA; zinc ribbon.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Binding Sites
  • Catalytic Domain
  • Humans
  • Models, Molecular
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Protein Domains
  • Protein Interaction Mapping
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism*
  • Sequence Homology, Amino Acid

Substances

  • NOB1 protein, human
  • Nuclear Proteins
  • PNO1 protein, human
  • RNA-Binding Proteins

Grants and funding

This work was supported by the Agence Nationale de la Recherche [ANR-16-CE11-0029]; Agence Nationale de la Recherche [ANR-10-BLAN-1224].